{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T03:53:56Z","timestamp":1788407636480,"version":"build-2803163510"},"reference-count":486,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2025,4,5]],"date-time":"2025-04-05T00:00:00Z","timestamp":1743811200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Microorganisms"],"abstract":"<jats:p>Streptococcus pneumoniae (pneumococcus) is a significant human pathogen responsible for a range of diseases from mild infections to invasive pneumococcal diseases, particularly affecting children, the elderly, and immunocompromised individuals. Despite pneumococcal conjugate vaccines having reduced disease incidence, challenges persist due to serotype diversity, vaccine coverage gaps, and antibiotic resistance. This review highlights the role of LytA, a key autolysin (N-acetylmuramoyl-l-alanine amidase), in pneumococcal biology. LytA regulates autolysis, contributes to inflammation, and biofilm formation, and impairs bacterial clearance. It also modulates complement activation, aiding immune evasion. LytA expression is influenced by environmental signals and genetic regulation and is tied to competence for genetic transformation, which is an important virulence trait, particularly in meningitis. With the increase in antibiotic resistance, LytA has emerged as a potential therapeutic target. Current research explores its use in bacteriolytic therapies, vaccine development, and synergistic antibiotic strategies. Various compounds, including synthetic peptides, plant extracts, and small molecules, have been investigated for their ability to trigger LytA-mediated bacterial lysis. Future directions include the development of novel anti-pneumococcal interventions leveraging LytA\u2019s properties while overcoming vaccine efficacy and resistance-related challenges. Human challenge models and animal studies continue to deepen our understanding of pneumococcal pathogenesis and potential treatment strategies.<\/jats:p>","DOI":"10.3390\/microorganisms13040827","type":"journal-article","created":{"date-parts":[[2025,4,10]],"date-time":"2025-04-10T10:47:41Z","timestamp":1744282061000},"page":"827","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Structure, Function, and Regulation of LytA: The N-Acetylmuramoyl-l-alanine Amidase Driving the \u201cSuicidal Tendencies\u201d of Streptococcus pneumoniae\u2014A Review"],"prefix":"10.3390","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1741-5486","authenticated-orcid":false,"given":"Ernesto","family":"Garc\u00eda","sequence":"first","affiliation":[{"name":"Centro de Investigaciones Biol\u00f3gicas Margarita Salas, Consejo Superior de Investigaciones Cient\u00edficas, 28040 Madrid, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,4,5]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/S1473-3099(04)00938-7","article-title":"Streptococcus pneumoniae colonisation: The key to pneumococcal disease","volume":"4","author":"Bogaert","year":"2004","journal-title":"Lancet Infect. Dis."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1586\/erv.12.53","article-title":"The fundamental link between pneumococcal carriage and disease","volume":"11","author":"Simell","year":"2012","journal-title":"Expert Rev. Vaccines"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1038\/s41564-018-0147-1","article-title":"Intracellular replication of Streptococcus pneumoniae inside splenic macrophages serves as a reservoir for septicaemia","volume":"3","author":"Ercoli","year":"2018","journal-title":"Nat. Microbiol."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Brissac, T., Mart\u00ednez, E., Kruckow Katherine, L., Riegler Ashleigh, N., Ganaie, F., Im, H., Bakshi, S., Arroyo-Diaz Nicole, M., Spencer Brady, L., and Saad Jamil, S. (2021). Capsule promotes intracellular survival and vascular endothelial cell translocation during invasive pneumococcal disease. mBio, 12.","DOI":"10.1128\/mBio.02516-21"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Hernandez-Morfa, M., Olivero, N.B., Zappia, V.E., Pi\u00f1as, G.E., Reinoso-Vizcaino, N.M., Cian, M.B., Nu\u00f1ez-Fernandez, M., Cortes, P.R., and Echenique, J. (2023). The oxidative stress response of Streptococcus pneumoniae: Its contribution to both extracellular and intracellular survival. Front. Microbiol., 14.","DOI":"10.3389\/fmicb.2023.1269843"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1111\/1348-0421.13060","article-title":"Molecular mechanism of Streptococcus pneumoniae-targeting xenophagy recognition and evasion: Reinterpretation of pneumococci as intracellular bacteria","volume":"67","author":"Ogawa","year":"2023","journal-title":"Microbiol. Immunol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"jcs260891","DOI":"10.1242\/jcs.260891","article-title":"Estimates of differential toxin expression governing heterogeneous intracellular lifespans of Streptococcus pneumoniae","volume":"137","author":"Santra","year":"2024","journal-title":"J. Cell Sci."},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Hernandez-Morfa, M., Reinoso-Vizcaino, N.M., Zappia, V.E., Olivero, N.B., Cortes, P.R., Stempin, C.C., Perez, D.R., and Echenique, J. (2024). Intracellular Streptococcus pneumoniae develops enhanced fluoroquinolone persistence during influenza A coinfection. Front. Microbiol., 15.","DOI":"10.3389\/fmicb.2024.1423995"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"e2424802","DOI":"10.1001\/jamanetworkopen.2024.24802","article-title":"Global case fatality of bacterial meningitis during an 80-year period: A systematic review and meta-analysis","volume":"7","author":"Liechti","year":"2024","journal-title":"JAMA Netw. Open"},{"key":"ref_10","unstructured":"Brown, J., Hammerschmidt, S., and Orihuela, C. (2015). Nasopharyngeal colonization with Streptococcus pneumoniae. Streptococcus pneumoniae: Molecular Mechanisms of Host-Pathogen Interactions, Academic Press."},{"key":"ref_11","unstructured":"GBD 2021 Lower Respiratory Infections and Antimicrobial Resistance Collaborators (2024). Global, regional, and national incidence and mortality burden of non-COVID-19 lower respiratory infections and aetiologies, 1990\u20132021: A systematic analysis from the Global Burden of Disease Study 2021. Lancet Infect. Dis., 24, 974\u20131002."},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Bennett, J.C., Knoll, M.D., Kagucia, E.W., Garcia Quesada, M., Zeger, S.L., Hetrich, M.K., Yang, Y., Herbert, C., Ogyu, A., and Cohen, A.L. (2025). Global impact of ten-valent and 13-valent pneumococcal conjugate vaccines on invasive pneumococcal disease in all ages (the PSERENADE project): A global surveillance analysis. Lancet Infect. Dis.","DOI":"10.2139\/ssrn.4763116"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"3028","DOI":"10.1016\/j.vaccine.2023.03.063","article-title":"A systematic review of pneumococcal conjugate vaccine impact on pneumococcal nasopharyngeal colonisation density in children under 5 years of age","volume":"41","author":"Jagne","year":"2023","journal-title":"Vaccine"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1080\/14760584.2022.2012455","article-title":"A systematic review of invasive pneumococcal disease vaccine failures and breakthrough with higher-valency pneumococcal conjugate vaccines in children","volume":"21","author":"Mungall","year":"2022","journal-title":"Expert Rev. Vaccines"},{"key":"ref_15","unstructured":"World Health Organization (WHO) (2025, February 26). Immunization Coverage. Available online: https:\/\/www.who.int\/news-room\/fact-sheets\/detail\/immunization-coverage#:~:text=Pneumococcal%20vaccine%20had%20been%20introduced,the%20WHO%20Western%20Pacific%20Region."},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Loughran, A.J., Orihuela, C.J., and Tuomanen, E.I. (2019). Streptococcus pneumoniae: Invasion and inflammation. Microbiol. Spectr., 7.","DOI":"10.1128\/microbiolspec.GPP3-0004-2018"},{"key":"ref_17","unstructured":"GBD 2021 Antimicrobial Resistance Collaborators (2024). Global burden of bacterial antimicrobial resistance 1990\u20132021: A systematic analysis with forecasts to 2050. Lancet, 404, 1199\u20131226."},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Rajput, P., Nahar, K.S., and Rahman, K.M. (2024). Evaluation of antibiotic resistance mechanisms in Gram-positive bacteria. Antibiotics, 13.","DOI":"10.3390\/antibiotics13121197"},{"key":"ref_19","unstructured":"World Health Organization (WHO) (2025, February 26). Bacterial Priority Pathogens List. Available online: https:\/\/iris.who.int\/bitstream\/handle\/10665\/376776\/9789240093461-eng.pdf?sequence=1."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1093\/femsre\/fux037","article-title":"A visual review of the human pathogen Streptococcus pneumoniae","volume":"41","author":"Engholm","year":"2017","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Brooks, L.R.K., and Mias, G.I. (2018). Streptococcus pneumoniae\u2019s virulence and host immunity: Aging, diagnostics, and prevention. Front. Immunol., 9.","DOI":"10.3389\/fimmu.2018.01366"},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Santoro, F., Iannelli, F., and Pozzi, G. (2019). Genomics and genetics of Streptococcus pneumoniae. Microbiol. Spectr., 7.","DOI":"10.1128\/microbiolspec.GPP3-0025-2018"},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Subramanian, K., Henriques-Normark, B., and Normark, S. (2019). Emerging concepts in the pathogenesis of the Streptococcus pneumoniae: From nasopharyngeal colonizer to intracellular pathogen. Cell. Microbiol., 21.","DOI":"10.1111\/cmi.13077"},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Morimura, A., Hamaguchi, S., Akeda, Y., and Tomono, K. (2021). Mechanisms underlying pneumococcal transmission and factors influencing host-pneumococcus interaction: A review. Front. Cell. Infect. Microbiol., 11.","DOI":"10.3389\/fcimb.2021.639450"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1186\/s41479-022-00097-y","article-title":"The remarkable history of pneumococcal vaccination: An ongoing challenge","volume":"14","author":"Musher","year":"2022","journal-title":"Pneumonia"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Neal, E.F.G., Chan, J., Nguyen, C.D., and Russell, F.M. (2022). Factors associated with pneumococcal nasopharyngeal carriage: A systematic review. PLoS Glob. Public Health, 2.","DOI":"10.1371\/journal.pgph.0000327"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1038\/s41541-023-00715-w","article-title":"Emerging vaccine strategies against the incessant pneumococcal disease","volume":"8","author":"Duke","year":"2023","journal-title":"npj Vaccines"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1046\/j.1365-2958.2001.02597.x","article-title":"The promoter of the operon encoding the F0F1 ATPase of Streptococcus pneumoniae is inducible by pH","volume":"41","year":"2001","journal-title":"Mol. Microbiol."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Li, L., Ma, J., Yu, Z., Li, M., Zhang, W., and Sun, H. (2023). Epidemiological characteristics and antibiotic resistance mechanisms of Streptococcus pneumoniae: An updated review. Microbiol. Res., 266.","DOI":"10.1016\/j.micres.2022.127221"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1097\/QCO.0000000000001005","article-title":"Epidemiology of community-acquired pneumonia caused by Streptococcus pneumoniae in older adults: A narrative review","volume":"37","author":"Elias","year":"2024","journal-title":"Curr. Opin. Infect. Dis."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"2409510","DOI":"10.1080\/21645515.2024.2409510","article-title":"Clinical and economic burden of otitis media in children under 5 years of age in the United States: A retrospective study","volume":"20","author":"Derreumaux","year":"2024","journal-title":"Hum. Vaccines Immunother."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/j.chembiol.2023.11.003","article-title":"Convergent impact of vaccination and antibiotic pressures on pneumococcal populations","volume":"31","author":"Johnson","year":"2024","journal-title":"Cell Chem. Biol."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Ricci Conesa, H., Skroder, H., Norton, N., Bencina, G., and Tsoumani, E. (2024). Clinical and economic burden of acute otitis media caused by Streptococcus pneumoniae in European children, after widespread use of PCVs-A systematic literature review of published evidence. PLoS ONE, 19.","DOI":"10.1371\/journal.pone.0297098"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1282","DOI":"10.1001\/jama.2024.14796","article-title":"Community-acquired pneumonia: A review","volume":"332","author":"Vaughn","year":"2024","journal-title":"JAMA"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"e0005924","DOI":"10.1128\/jb.00059-24","article-title":"Biological puzzles solved by using Streptococcus pneumoniae: A historical review of the pneumococcal studies that have impacted medicine and shaped molecular bacteriology","volume":"206","author":"Hiller","year":"2024","journal-title":"J. Bacteriol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1038\/s41579-024-01116-z","article-title":"Streptococcus pneumoniae epidemiology, pathogenesis and control","volume":"23","author":"Narciso","year":"2024","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"e00175-24","DOI":"10.1128\/cmr.00175-24","article-title":"Update on the evolving landscape of pneumococcal capsule types: New discoveries and way forward","volume":"38","author":"Ganaie","year":"2025","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_38","first-page":"159","article-title":"Sur une maladie nouvelle, provoqu\u00e9e par la salive d\u2019un enfant mort de la rage","volume":"92","author":"Pasteur","year":"1881","journal-title":"Compt. Rend. Acad. Sci."},{"key":"ref_39","first-page":"781","article-title":"A fatal form of septicaemia in the rabbit, produced by the subcutaneous injection of human saliva. An experimental research","volume":"2","author":"Sternberg","year":"1881","journal-title":"Natl. Board Health Bull."},{"key":"ref_40","unstructured":"(1890). Report of Dr. Welch\u2019s remarks on the Diplococcus pneumoniae at the meeting of the John Hopkins Hospital Medical Society, on February 17, 1890. Johns Hopkins Hosp. Bull., I, 73\u201374. Available online: https:\/\/babel.hathitrust.org\/cgi\/pt?id=iau.31858029237678&seq=80."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1007\/BF02140459","article-title":"Ueber eine specifische bakteriolystische wirkung der galle","volume":"34","author":"Neufeld","year":"1900","journal-title":"Z. Hyg. Infektionskrankh."},{"key":"ref_42","unstructured":"White, B., Robinson, E.S., and Barnes, L.A. (1979). The Biology of Pneumococcus: The Bacteriological, Biochemical, and Immunological Characters and Activities of Diplococcus pneumoniae, Harvard University Press."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"S331","DOI":"10.1093\/cid\/cir048","article-title":"Interpreting assays for the detection of Streptococcus pneumoniae","volume":"52","author":"Blaschke","year":"2011","journal-title":"Clin. Infect. Dis."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.vaccine.2013.08.062","article-title":"Standard method for detecting upper respiratory carriage of Streptococcus pneumoniae: Updated recommendations from the World Health Organization Pneumococcal Carriage Working Group","volume":"32","author":"Satzke","year":"2013","journal-title":"Vaccine"},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Slotved, H.-C., Facklam, R.R., and Fuursted, K. (2017). Assessment of a novel bile solubility test and MALDI-TOF for the differentiation of Streptococcus pneumoniae from other mitis group streptococci. Sci. Rep., 7.","DOI":"10.1038\/s41598-017-07772-x"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Aupaix, A., Verroken, A., and Rodriguez-Villalobos, H. (2024). Evaluation of a new protocol for rapid identification of Streptococcus pneumoniae in blood cultures using the modified bile solubility test: Gram staining is still standing. J. Clin. Microbiol., 63.","DOI":"10.1128\/jcm.01222-24"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"e0046321","DOI":"10.1128\/IAI.00463-21","article-title":"Prophylactic inhibition of colonization by Streptococcus pneumoniae with the secondary bile acid metabolite deoxycholic acid","volume":"89","author":"Vidal","year":"2021","journal-title":"Infect. Immun."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1943","DOI":"10.1001\/jama.1910.02550500029014","article-title":"The autolysis of pneumococci and the effect of the injection of autolyzed pneumococci","volume":"54","author":"Rosenow","year":"1910","journal-title":"JAMA"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1084\/jem.38.2.199","article-title":"Studies on the enzymes of pneumococcus. IV. Bacteriolytic enzyme","volume":"38","author":"Avery","year":"1923","journal-title":"J. Exp. Med."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1084\/jem.65.6.873","article-title":"The autolytic system of pneumococci","volume":"65","author":"Dubos","year":"1937","journal-title":"J. Exp. Med."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1073\/pnas.59.1.86","article-title":"Biological consequences of the replacement of choline by ethanolamine in the cell wall of Pneumococcus: Chain formation, loss of transformability, and loss of autolysis","volume":"59","author":"Tomasz","year":"1968","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Warrier, I., Perry, A., Hubbell, S.M., Eichelman, M., van Opijnen, T., and Meyer, M.M. (2024). RNA cis-regulators are important for Streptococcus pneumoniae in vivo success. PLoS Genet., 20.","DOI":"10.1371\/journal.pgen.1011188"},{"key":"ref_53","unstructured":"McCarty, M. (1985). The Transforming Principle. Discovering That Genes Are Made of DNA, W. W. Norton & Co."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"6532","DOI":"10.1128\/JB.00813-07","article-title":"SpxB Is a suicide gene of Streptococcus pneumoniae and confers a selective advantage in an in vivo competitive colonization model","volume":"189","author":"Trzcinski","year":"2007","journal-title":"J. Bacteriol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1046\/j.1469-0691.2000.00172.x","article-title":"Apparently false-positive blood cultures due to autolyzed Streptococcus pneumoniae","volume":"6","author":"Vasallo","year":"2000","journal-title":"Clin. Microbiol. Infect."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"e00055-22","DOI":"10.1128\/spectrum.00055-22","article-title":"Characteristics of false-positive alarms in the BacT\/Alert 3D system","volume":"10","author":"Amano","year":"2022","journal-title":"Microbiol. Spectr."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1038\/227138a0","article-title":"Multiple antibiotic resistance in a bacterium with suppressed autolytic system","volume":"227","author":"Tomasz","year":"1970","journal-title":"Nature"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1146\/annurev.mi.33.100179.000553","article-title":"The mechanism of the irreversible antimicrobial effects of penicillins: How the beta-lactam antibiotics kill and lyse bacteria","volume":"33","author":"Tomasz","year":"1979","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1111\/j.1432-1033.1986.tb09749.x","article-title":"Searching for autolysin functions. Characterization of a pneumococcal mutant deleted in the lytA gene","volume":"158","author":"Ronda","year":"1986","journal-title":"Eur. J. Biochem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1111\/j.1432-1033.1987.tb11172.x","article-title":"Biological role of the pneumococcal amidase. Cloning of the lytA gene in Streptococcus pneumoniae","volume":"164","author":"Ronda","year":"1987","journal-title":"Eur. J. Biochem."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1159\/000220828","article-title":"Quinolones with enhanced bactericidal activity induce autolysis in Streptococcus pneumoniae","volume":"55","author":"Okumura","year":"2009","journal-title":"Chemotherapy"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1016\/j.jiac.2018.09.012","article-title":"Gene expression analysis in the potent bactericidal activity of sitafloxacin against Streptococcus pneumoniae","volume":"25","author":"Kobayashi","year":"2019","journal-title":"J. Infect. Chemother."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1136\/jcp.40.4.368","article-title":"Evaluation of anaerobic culture and effect of culture medium supplementation with factor V on colonial morphology and efficacy of isolation of Streptococcus pneumoniae from sputum","volume":"40","author":"Brogan","year":"1987","journal-title":"J. Clin. Pathol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1545","DOI":"10.1093\/infdis\/jiy718","article-title":"Effects of anaerobic culturing on pathogenicity and virulence-related gene-expression in pneumococcal pneumonia","volume":"219","author":"Nagaoka","year":"2018","journal-title":"J. Infect. Dis."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/S0021-9258(18)63393-9","article-title":"Choline-containing teichoic acid as a structural component of pneumococcal cell wall and its role in sensitivity to lysis by an autolytic enzyme","volume":"245","author":"Mosser","year":"1970","journal-title":"J. Biol. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1128\/jb.117.2.796-804.1974","article-title":"Specificity of the autolysin of Streptococcus (Diplococcus) pneumoniae","volume":"117","author":"Howard","year":"1974","journal-title":"J. Bacteriol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1007\/BF00425663","article-title":"Cloning and expression of the pneumococcal autolysin gene in Escherichia coli","volume":"201","author":"Ronda","year":"1985","journal-title":"Mol. Gen. Genet."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/0378-1119(86)90215-5","article-title":"Nucleotide sequence and expression of the pneumococcal autolysin gene from its own promoter in Escherichia coli","volume":"43","year":"1986","journal-title":"Gene"},{"key":"ref_69","first-page":"133","article-title":"Preparation of antiserum against the pneumococcal autolysin\u2014Inhibition of autolysin activity and some autolytic processes by the antibody","volume":"14","author":"Rojo","year":"1982","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_70","doi-asserted-by":"crossref","unstructured":"Miellet, W.R., Almeida, S.T., Trzci\u0144ski, K., and S\u00e1-Le\u00e3o, R. (2023). Streptococcus pneumoniae carriage studies in adults: Importance, challenges, and key issues to consider when using quantitative PCR-based approaches. Front. Microbiol., 14.","DOI":"10.3389\/fmicb.2023.1122276"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1046\/j.1365-2958.1999.01455.x","article-title":"The molecular characterization of the first autolytic lysozyme of Streptococcus pneumoniae reveals evolutionary mobile domains","volume":"33","year":"1999","journal-title":"Mol. Microbiol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"28618","DOI":"10.1074\/jbc.M802808200","article-title":"Insights into the structure-function relationships of pneumococcal cell wall lysozymes, LytC and Cpl-1","volume":"283","author":"Monterroso","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1111\/j.1574-6968.1986.tb01520.x","article-title":"A new peptidoglycan hydrolase in Streptococcus pneumoniae","volume":"35","author":"Ronda","year":"1986","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1111\/j.1574-6968.1990.tb04019.x","article-title":"Autolysins are direct involved in the bactericidal effect caused by penicillin in wild type and in tolerant pneumococci","volume":"66","author":"Ronda","year":"1990","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1046\/j.1365-2273.2002.00544.x","article-title":"Nasal mucosal temperature during respiration","volume":"27","author":"Lindemann","year":"2002","journal-title":"Clin. Otolaryngol. Allied Sci."},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"V\u00e1zquez, R., and Briers, Y. (2023). What\u2019s in a name? An overview of the proliferating nomenclature in the field of phage lysins. Cells, 12.","DOI":"10.3390\/cells12152016"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1111\/j.1365-2958.2004.04305.x","article-title":"Release of DNA into the medium by competent Streptococcus pneumoniae: Kinetics, mechanism and stability of the liberated DNA","volume":"54","author":"Moscoso","year":"2004","journal-title":"Mol. Microbiol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"8710","DOI":"10.1073\/pnas.0500879102","article-title":"Competence-programmed predation of noncompetent cells in the human pathogen Streptococcus pneumoniae: Genetic requirements","volume":"102","author":"Guiral","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"4338","DOI":"10.1128\/JB.187.13.4338-4345.2005","article-title":"Choline-binding protein D (CbpD) in Streptococcus pneumoniae is essential for competence-induced cell lysis","volume":"187","author":"Kausmally","year":"2005","journal-title":"J. Bacteriol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1111\/j.1365-2958.2010.07143.x","article-title":"Pneumococcal CbpD is a murein hydrolase that requires a dual cell envelope binding specificity to kill target cells during fratricide","volume":"76","author":"Eldholm","year":"2010","journal-title":"Mol. Microbiol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1297","DOI":"10.1111\/j.1365-2958.2005.05021.x","article-title":"New insights into the pneumococcal fratricide: Relationship to clumping and identification of a novel immunity factor","volume":"59","author":"Martin","year":"2006","journal-title":"Mol. Microbiol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1621","DOI":"10.1038\/s41467-017-01716-9","article-title":"A programmed cell division delay preserves genome integrity during natural genetic transformation in Streptococcus pneumoniae","volume":"8","author":"Mercy","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"2223","DOI":"10.1099\/mic.0.026328-0","article-title":"Fratricide in Streptococcus pneumoniae: Contributions and role of the cell wall hydrolases CbpD, LytA and LytC","volume":"155","author":"Eldholm","year":"2009","journal-title":"Microbiology"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/j.meegid.2014.10.020","article-title":"Natural transformation and genome evolution in Streptococcus pneumoniae","volume":"33","author":"Straume","year":"2015","journal-title":"Infect. Genet. Evol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"5897","DOI":"10.1128\/AEM.01343-12","article-title":"Fratricide is essential for efficient gene transfer between pneumococci in biofilms","volume":"78","author":"Wei","year":"2012","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1111\/mmi.13016","article-title":"Deletion analysis of Streptococcus pneumoniae late competence genes distinguishes virulence determinants that are dependent or independent of competence induction","volume":"97","author":"Zhu","year":"2015","journal-title":"Mol. Microbiol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1093\/infdis\/151.5.859","article-title":"The induction of meningeal inflammation by components of the pneumococcal cell wall","volume":"151","author":"Tuomanen","year":"1985","journal-title":"J. Infect. Dis."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1093\/infdis\/151.3.535","article-title":"The relative role of bacterial cell wall and capsule in the induction of inflammation in pneumococcal meningitis","volume":"151","author":"Tuomanen","year":"1985","journal-title":"J. Infect. Dis."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1007\/BF02013304","article-title":"Induction of meningeal inflammation by diverse bacterial cell walls","volume":"5","author":"Tuomanen","year":"1986","journal-title":"Eur. J. Clin. Microbiol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1177\/00034894880970S308","article-title":"Contribution of pneumococcal cell wall to experimental otitis media pathogenesis","volume":"132","author":"Giebink","year":"1988","journal-title":"Ann. Otol. Rhinol. Laryngol. Suppl."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1093\/infdis\/157.2.245","article-title":"The contribution of pneumococcal cell wall to the pathogenesis of experimental otitis media","volume":"157","author":"Giebink","year":"1988","journal-title":"J. Infect. Dis."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1128\/iai.64.4.1140-1145.1996","article-title":"Roles of autolysin and pneumolysin in middle ear inflammation caused by a type 3 Streptococcus pneumoniae strain in the chinchilla otitis media model","volume":"64","author":"Sato","year":"1996","journal-title":"Infect. Immun."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"12537","DOI":"10.1074\/jbc.274.18.12537","article-title":"Digestion of Streptococcus pneumoniae cell walls with its major peptidoglycan hydrolase releases branched stem peptides carrying proinflammatory activity","volume":"274","author":"Majcherczyk","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1040","DOI":"10.1086\/378238","article-title":"Penicillin enhances the Toll-like receptor 2-mediated proinflammatory activity of Streptococcus pneumoniae","volume":"188","author":"Moore","year":"2003","journal-title":"J. Infect. Dis."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1080\/00365540310016259","article-title":"Proinflammatory activity of cell-wall constituents from gram-positive bacteria","volume":"35","author":"Moreillon","year":"2003","journal-title":"Scand. J. Infect. Dis."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"490346","DOI":"10.1155\/2013\/490346","article-title":"Overview of community-acquired pneumonia and the role of inflammatory mechanisms in the immunopathogenesis of severe pneumococcal disease","volume":"2013","author":"Steel","year":"2013","journal-title":"Mediat. Inflamm."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.cellimm.2018.01.006","article-title":"Pneumococcal DNA-binding proteins released through autolysis induce the production of proinflammatory cytokines via toll-like receptor 4","volume":"325","author":"Nagai","year":"2018","journal-title":"Cell. Immunol."},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"Wall, E.C., Brownridge, P., Laing, G., Terra, V.S., Mlozowa, V., Denis, B., Nyirenda, M., Allain, T., Ramos-Sevillano, E., and Carrol, E. (2020). CSF levels of elongation factor Tu is associated with increased mortality in Malawian adults with Streptococcus pneumoniae meningitis. Front. Cell. Infect. Microbiol., 10.","DOI":"10.3389\/fcimb.2020.603623"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1186\/s41479-023-00110-y","article-title":"Acute organ injury and long-term sequelae of severe pneumococcal infections","volume":"15","author":"Kruckow","year":"2023","journal-title":"Pneumonia"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"7785","DOI":"10.1128\/JB.00673-06","article-title":"Biofilm formation by Streptococcus pneumoniae: Role of choline, extracellular DNA, and capsular polysaccharide in microbial accretion","volume":"188","author":"Moscoso","year":"2006","journal-title":"J. Bacteriol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1111\/j.1751-7915.2011.00294.x","article-title":"Biofilm formation in Streptococcus pneumoniae","volume":"5","author":"Domenech","year":"2012","journal-title":"Microb. Biotechnol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1111\/j.1462-2920.2012.02853.x","article-title":"Insight into the composition of the intercellular matrix of Streptococcus pneumoniae biofilms","volume":"15","author":"Domenech","year":"2013","journal-title":"Environ. Microbiol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1111\/1758-2229.12295","article-title":"In vitro biofilm development of Streptococcus pneumoniae and formation of choline-binding protein\u2013DNA complexes","volume":"7","author":"Domenech","year":"2015","journal-title":"Environ. Microbiol. Rep."},{"key":"ref_104","doi-asserted-by":"crossref","unstructured":"Brown, L.R., Caulkins, R.C., Schartel, T.E., Rosch, J.W., Honsa, E.S., Schultz-Cherry, S., Meliopoulos, V.A., Cherry, S., and Thornton, J.A. (2017). Increased zinc availability enhances initial aggregation and biofilm formation of Streptococcus pneumoniae. Front. Cell. Infect. Microbiol., 7.","DOI":"10.3389\/fcimb.2017.00233"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"e00154-23","DOI":"10.1128\/iai.00154-23","article-title":"The choline-binding proteins PspA, PspC, and LytA of Streptococcus pneumoniae and their interaction with human endothelial and red blood cells","volume":"91","author":"Vilhena","year":"2023","journal-title":"Infect. Immun."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"3826","DOI":"10.1128\/IAI.00290-09","article-title":"Streptococcus pneumoniae autolysis prevents phagocytosis and production of phagocyte-activating cytokines","volume":"77","author":"Martner","year":"2009","journal-title":"Infect. Immun."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"e00960-16","DOI":"10.1128\/IAI.00960-16","article-title":"Intact pneumococci trigger transcription of interferon-related genes in human monocytes, while fragmented, autolyzed bacteria subvert this response","volume":"85","author":"Skovbjerg","year":"2017","journal-title":"Infect. Immun."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1128\/jvi.21.1.366-374.1977","article-title":"Role of the pneumococcal autolysin (murein hydrolase) in the release of phage progeny bacteriophage and in the bacteriophage-induced lysis of the host cells","volume":"21","author":"Lopez","year":"1977","journal-title":"J. Virol."},{"key":"ref_109","first-page":"479","article-title":"Mechanism of phage-induced lysis in pneumococci","volume":"129","author":"Garcia","year":"1983","journal-title":"J. Gen. Microbiol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"5428","DOI":"10.1128\/JB.00477-09","article-title":"The autolysin LytA contributes to efficient bacteriophage progeny release in Streptococcus pneumoniae","volume":"191","author":"Frias","year":"2009","journal-title":"J. Bacteriol."},{"key":"ref_111","unstructured":"Frias, M.J.R. (2011). Lysis Strategy of Streptococcus pneumoniae Bacteriophages: Mechanisms and Host Implication. [Ph.D. Thesis, Universidade de Lisboa]. Available online: https:\/\/repositorio.ul.pt\/bitstream\/10451\/4644\/3\/ulsd061521_td_Maria_Frias.pdf."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1111\/mmi.12108","article-title":"Export of the pneumococcal phage SV1 lysin requires choline-containing teichoic acids and is holin-independent","volume":"87","author":"Frias","year":"2013","journal-title":"Mol. Microbiol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"2747","DOI":"10.1093\/gbe\/evv178","article-title":"Insights into the evolutionary relationships of LytA autolysin and Ply pneumolysin-like genes in Streptococcus pneumoniae and related streptococci","volume":"7","author":"Morales","year":"2015","journal-title":"Genome Biol. Evol."},{"key":"ref_114","doi-asserted-by":"crossref","unstructured":"Nishimoto, A.T., Rosch, J.W., and Tuomanen, E.I. (2020). Pneumolysin: Pathogenesis and therapeutic target. Front. Microbiol., 11.","DOI":"10.3389\/fmicb.2020.01543"},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Pereira, J.M., Xu, S., Leong, J.M., and Sousa, S. (2022). The Yin and Yang of pneumolysin during pneumococcal infection. Front. Immunol., 13.","DOI":"10.3389\/fimmu.2022.878244"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1046\/j.1365-2958.1998.00732.x","article-title":"Membrane targeting of RecA during genetic transformation","volume":"27","author":"Masure","year":"1998","journal-title":"Mol. Microbiol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1111\/j.1365-2958.1995.tb02250.x","article-title":"The recA gene of Streptococcus pneumoniae is part of a competence-induced operon and controls lysogenic induction","volume":"15","author":"Martin","year":"1995","journal-title":"Mol. Microbiol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1128\/jb.177.1.86-93.1995","article-title":"The rec locus, a competence-induced operon in Streptococcus pneumoniae","volume":"177","author":"Pearce","year":"1995","journal-title":"J. Bacteriol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1128\/AAC.01298-12","article-title":"Functional analysis of pneumococcal drug efflux pumps associates the MATE DinF transporter with quinolone susceptibility","volume":"57","author":"Tocci","year":"2013","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_120","first-page":"1389","article-title":"Large-scale identification of serotype 4 Streptococcus pneumoniae virulence factors","volume":"45","author":"Hava","year":"2002","journal-title":"Mol. Microbiol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/0378-1119(90)90454-Y","article-title":"Characterization of the transcription unit encoding the major pneumococcal autolysin","volume":"90","year":"1990","journal-title":"Gene"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1046\/j.1365-2958.1998.00668.x","article-title":"Competence-specific induction of recA is required for full recombination proficiency during transformation in Streptococcus pneumoniae","volume":"27","author":"Claverys","year":"1998","journal-title":"Mol. Microbiol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1046\/j.1365-2958.1998.00737.x","article-title":"A competence regulon in Streptococcus pneumoniae revealed by genomic analysis","volume":"27","author":"Campbell","year":"1998","journal-title":"Mol. Microbiol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"2701","DOI":"10.1128\/JB.180.10.2701-2710.1998","article-title":"Isolation and characterization of three Streptococcus pneumoniae transformation-specific loci by use of a lacZ reporter insertion vector","volume":"180","author":"Pestova","year":"1998","journal-title":"J. Bacteriol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"5004","DOI":"10.1128\/JB.181.16.5004-5016.1999","article-title":"Identification of a new regulator in Streptococcus pneumoniae linking quorum sensing to competence for genetic transformation","volume":"181","author":"Lee","year":"1999","journal-title":"J. Bacteriol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1128\/JB.185.1.349-358.2003","article-title":"Transient association of an alternative sigma factor, ComX, with RNA polymerase during the period of competence for genetic transformation in Streptococcus pneumoniae","volume":"185","author":"Luo","year":"2003","journal-title":"J. Bacteriol."},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Solano-Collado, V., Ruiz-Cruz, S., Lorenzo-D\u00edaz, F., Pluta, R., Espinosa, M., and Bravo, A. (2021). Recognition of streptococcal promoters by the pneumococcal SigA protein. Front. Mol. Biosci., 8.","DOI":"10.3389\/fmolb.2021.666504"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"3052","DOI":"10.1128\/JB.187.9.3052-3061.2005","article-title":"Two distinct functions of ComW in stabilization and activation of the alternative sigma factor ComX in Streptococcus pneumoniae","volume":"187","author":"Sung","year":"2005","journal-title":"J. Bacteriol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"2370","DOI":"10.1128\/JB.00354-16","article-title":"Competence for genetic transformation in Streptococcus pneumoniae: Mutations in \u03c3A bypass the ComW requirement for late gene expression","volume":"198","author":"Tovpeko","year":"2016","journal-title":"J. Bacteriol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"11101","DOI":"10.1074\/jbc.RA119.007571","article-title":"The pneumococcal \u03c3X activator, ComW, is a DNA-binding protein critical for natural transformation","volume":"294","author":"Inniss","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1038\/21202","article-title":"Emergence of vancomycin tolerance in Streptococcus pneumoniae","volume":"399","author":"Novak","year":"1999","journal-title":"Nature"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"1345","DOI":"10.4014\/jmb.1105.05045","article-title":"pep27 and lytA in vancomycin-tolerant pneumococci","volume":"21","author":"Olivares","year":"2011","journal-title":"J. Microbiol. Biotechnol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"e44912","DOI":"10.7554\/eLife.44912","article-title":"A switch in surface polymer biogenesis triggers growth-phase-dependent and antibiotic-induced bacteriolysis","volume":"8","author":"Dobihal","year":"2019","journal-title":"eLife"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1006\/jmbi.1995.0366","article-title":"An extended \u201310 promoter alone directs transcription of the DpnII operon of Streptococcus pneumoniae","volume":"250","author":"Sabelnikov","year":"1995","journal-title":"J. Mol. Biol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"e00780-18","DOI":"10.1128\/JB.00780-18","article-title":"Refining the pneumococcal competence regulon by RNA sequencing","volume":"201","author":"Slager","year":"2019","journal-title":"J. Bacteriol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"D839","DOI":"10.1093\/nar\/gkae923","article-title":"PneumoBrowse 2: An integrated visual platform for curated genome annotation and multiomics data analysis of Streptococcus pneumoniae","volume":"53","author":"Janssen","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"e00764-18","DOI":"10.1128\/JB.00764-18","article-title":"Redefining the small regulatory RNA transcriptome in Streptococcus pneumoniae serotype 2 strain D39","volume":"201","author":"Sinha","year":"2019","journal-title":"J. Bacteriol."},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Sinha, D., Frick Jacob, P., Clemons, K., Winkler, M.E., and De Lay, N.R. (2021). Pivotal roles for ribonucleases in Streptococcus pneumoniae pathogenesis. mBio, 12.","DOI":"10.1128\/mBio.02385-21"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"2100211","DOI":"10.1002\/pmic.202100211","article-title":"Microproteins\u2014Discovery, structure, and function","volume":"23","author":"Mohsen","year":"2023","journal-title":"Proteomics"},{"key":"ref_140","doi-asserted-by":"crossref","unstructured":"Simoens, L., Fijalkowski, I., and Van Damme, P. (2023). Exposing the small protein load of bacterial life. FEMS Microbiol. Rev., 47.","DOI":"10.1093\/femsre\/fuad063"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"e01247-22","DOI":"10.1128\/mbio.01247-22","article-title":"Discovery of unannotated small open reading frames in Streptococcus pneumoniae D39 involved in quorum sensing and virulence using ribosome profiling","volume":"13","author":"Laczkovich","year":"2022","journal-title":"mBio"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1016\/j.tibs.2023.09.002","article-title":"Two for one: Regulatory RNAs that encode small proteins","volume":"48","author":"Aoyama","year":"2023","journal-title":"Trends Biochem. Sci."},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Ferrara, S., Brignoli, T., and Bertoni, G. (2023). Little reason to call them small noncoding RNAs. Front. Microbiol., 14.","DOI":"10.3389\/fmicb.2023.1191166"},{"key":"ref_144","doi-asserted-by":"crossref","unstructured":"Jordan, B., Weidenbach, K., and Schmitz, R.A. (2023). The power of the small: The underestimated role of small proteins in bacterial and archaeal physiology. Curr. Opin. Microbiol., 76.","DOI":"10.1016\/j.mib.2023.102384"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"7563","DOI":"10.1038\/s41467-024-51894-6","article-title":"A catalog of small proteins from the global microbiome","volume":"15","author":"Duan","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"2627","DOI":"10.1073\/pnas.68.11.2627","article-title":"Abnormal autolytic enzyme in a pneumococcus with altered teichoic acid composition","volume":"68","author":"Tomasz","year":"1971","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"4199","DOI":"10.1016\/S0021-9258(17)33281-7","article-title":"Purification of the pneumococcal N-acetylmuramyl-l-alanine amidase to biochemical homogeneity","volume":"251","author":"Tomasz","year":"1976","journal-title":"J. Biol. Chem."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1128\/jb.158.3.1188-1190.1984","article-title":"Attachment of pneumococcal autolysin to wall teichoic acids, an essential step in enzymatic wall degradation","volume":"158","author":"Giudicelli","year":"1984","journal-title":"J. Bacteriol."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1111\/j.1432-1033.1985.tb08668.x","article-title":"Interaction of the pneumococcal amidase with lipoteichoic acid and choline","volume":"146","author":"Briese","year":"1985","journal-title":"Eur. J. Biochem."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/0014-5793(88)80759-2","article-title":"Structural requirements of choline derivatives for \u2018conversion\u2019 of pneumococcal amidase. A new single-step procedure for purification of this autolysin","volume":"232","author":"Sanz","year":"1988","journal-title":"FEBS Lett."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1016\/S0021-9258(18)73286-9","article-title":"Choline, pantothenic acid, and nicotinic acid as essential growth factors for pneumococcus","volume":"134","author":"Rane","year":"1940","journal-title":"J. Biol. Chem."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1089\/mdr.2012.0026","article-title":"Biosynthesis of teichoic acids in Streptococcus pneumoniae and closely related species: Lessons from genomes","volume":"18","author":"Denapaite","year":"2012","journal-title":"Microb. Drug Resist."},{"key":"ref_153","doi-asserted-by":"crossref","unstructured":"Vollmer, W., Massidda, O., and Tomasz, A. (2019). The cell wall of Streptococcus pneumoniae. Microbiol. Spectr., 7.","DOI":"10.1128\/microbiolspec.GPP3-0018-2018"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"2379","DOI":"10.1128\/JB.01795-07","article-title":"A new model of pneumococcal lipoteichoic acid structure resolves biochemical, biosynthetic, and serologic inconsistencies of the current model","volume":"190","author":"Seo","year":"2008","journal-title":"J. Bacteriol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"15654","DOI":"10.1074\/jbc.M112.446963","article-title":"Structural reevaluation of Streptococcus pneumoniae lipoteichoic acid and new insights into its immunostimulatory potency","volume":"288","author":"Gisch","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1128\/jb.169.2.447-453.1987","article-title":"Teichoic acid-containing muropeptides from Streptococcus pneumoniae as substrates for the pneumococcal autolysin","volume":"169","author":"Tomasz","year":"1987","journal-title":"J. Bacteriol."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1089\/mdr.1997.3.391","article-title":"Autolysis and cell wall degradation in a choline-independent strain of Streptococcus pneumoniae","volume":"3","author":"Severin","year":"1997","journal-title":"Microb. Drug Resist."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1046\/j.1365-2958.1996.399929.x","article-title":"The two-step lysis system of pneumococcal bacteriophage EJ-1 is functional in Gram-negative bacteria: Triggering of the major pneumococcal autolysin in Escherichia coli","volume":"19","author":"Munthali","year":"1996","journal-title":"Mol. Microbiol."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1128\/jb.171.1.114-119.1989","article-title":"Mechanisms of pneumococcal cell wall degradation in vitro and in vivo","volume":"171","author":"Tomasz","year":"1989","journal-title":"J. Bacteriol."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"D444","DOI":"10.1093\/nar\/gkae1082","article-title":"InterPro: The protein sequence classification resource in 2025","volume":"53","author":"Blum","year":"2025","journal-title":"Nucleic Acids Res."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1038\/nri.2017.136","article-title":"Peptidoglycan recognition by the innate immune system","volume":"18","author":"Wolf","year":"2018","journal-title":"Nat. Rev. Immunol."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"994","DOI":"10.1016\/j.bbrc.2006.09.139","article-title":"PGRP-SB1: An N-acetylmuramoyl L-alanine amidase with antibacterial activity","volume":"350","author":"Mellroth","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1111\/j.1462-5822.2006.00726.x","article-title":"Mammalian PGRPs: Novel antibacterial proteins","volume":"8","author":"Dziarski","year":"2006","journal-title":"Cell. Microbiol."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.molimm.2018.12.021","article-title":"Peptidoglycan recognition proteins in insect immunity","volume":"106","author":"Wang","year":"2019","journal-title":"Mol. Immunol."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.fsi.2020.02.013","article-title":"Identification and characterization of a novel short-type peptidoglycan recognition protein in Apostichopus japonicus","volume":"99","author":"Hu","year":"2020","journal-title":"Fish Shellfish Immunol."},{"key":"ref_166","doi-asserted-by":"crossref","unstructured":"Zhao, L., Niu, J., Feng, D., Wang, X., and Zhang, R. (2023). Immune functions of pattern recognition receptors in Lepidoptera. Front. Immunol., 14.","DOI":"10.3389\/fimmu.2023.1203061"},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1111\/j.1574-6976.2009.00172.x","article-title":"Versatility of choline metabolism and choline-binding proteins in Streptococcus pneumoniae and commensal streptococci","volume":"33","author":"Hakenbeck","year":"2009","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_168","doi-asserted-by":"crossref","unstructured":"Frolet, C., Beniazza, M., Roux, L., Gallet, B., Noirclerc-Savoye, M., Vernet, T., and Di Guilmi, A.M. (2010). New adhesin functions of surface-exposed pneumococcal proteins. BMC Microbiol., 10.","DOI":"10.1186\/1471-2180-10-190"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1111\/j.2041-1014.2012.00655.x","article-title":"Pneumococcal surface proteins: When the whole is greater than the sum of its parts","volume":"27","author":"Hermoso","year":"2012","journal-title":"Mol. Oral Microbiol."},{"key":"ref_170","doi-asserted-by":"crossref","unstructured":"Maestro, B., and Sanz, J.M. (2016). Choline binding proteins from Streptococcus pneumoniae: A dual role as enzybiotics and targets for the design of new antimicrobials. Antibiotics, 5.","DOI":"10.3390\/antibiotics5020021"},{"key":"ref_171","doi-asserted-by":"crossref","unstructured":"Aceil, J., and Avci, F.Y. (2022). Pneumococcal surface proteins as virulence factors, immunogens, and conserved vaccine targets. Front. Cell. Infect. Microbiol., 12.","DOI":"10.3389\/fcimb.2022.832254"},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"2573","DOI":"10.1128\/jvi.61.8.2573-2580.1987","article-title":"Cloning, purification, and biochemical characterization of the pneumococcal bacteriophage Cp-1 lysin","volume":"61","author":"Ronda","year":"1987","journal-title":"J. Virol."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/0378-1119(90)90116-9","article-title":"Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages","volume":"86","year":"1990","journal-title":"Gene"},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"8125","DOI":"10.1073\/pnas.87.20.8125","article-title":"Chimeric phage-bacterial enzymes: A clue to the modular evolution of genes","volume":"87","year":"1990","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/0014-5793(93)81621-6","article-title":"Role of the C-terminal domain of the lysozyme of Clostridium acetobutylicum ATCC 824 in a chimeric pneumococcal-clostridial cell wall lytic enzyme","volume":"336","author":"Croux","year":"1993","journal-title":"FEBS Lett."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1111\/j.1365-2958.1993.tb01231.x","article-title":"Interchange of functional domains switches enzyme specificity: Construction of a chimeric pneumococcal-clostridial cell wall lytic enzyme","volume":"9","author":"Croux","year":"1993","journal-title":"Mol. Microbiol."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/0378-1119(90)90207-8","article-title":"Cloning and expression of gene fragments encoding the choline-binding domain of pneumococcal murein hydrolases","volume":"89","author":"Sanz","year":"1990","journal-title":"Gene"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"4066","DOI":"10.1128\/jb.176.13.4066-4072.1994","article-title":"Carboxy-terminal deletion analysis of the major pneumococcal autolysin","volume":"176","author":"Garcia","year":"1994","journal-title":"J. Bacteriol."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"6832","DOI":"10.1074\/jbc.271.12.6832","article-title":"Structural organization of the major autolysin from Streptococcus pneumoniae","volume":"271","author":"Usobiaga","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1093\/protein\/gzq087","article-title":"Structural autonomy of a \u03b2-hairpin peptide derived from the pneumococcal choline-binding protein LytA","volume":"24","author":"Maestro","year":"2011","journal-title":"Protein Eng. Des. Sel."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1016\/j.ijbiomac.2021.08.223","article-title":"Inter-hairpin linker sequences determine the structure of the \u03b2\u03b2-solenoid fold: A \u201cbottom-up\u201d study of pneumococcal LytA choline-binding module","volume":"190","author":"Maestro","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1016\/j.tibs.2004.09.006","article-title":"The power of two: Protein dimerization in biology","volume":"29","author":"Marianayagam","year":"2004","journal-title":"Trends Biochem. Sci."},{"key":"ref_183","doi-asserted-by":"crossref","unstructured":"Dang, D.T. (2022). Molecular approaches to protein dimerization: Opportunities for supramolecular chemistry. Front. Chem., 10.","DOI":"10.3389\/fchem.2022.829312"},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.1128\/JCM.40.7.2545-2554.2002","article-title":"Molecular peculiarities of the lytA gene isolated from clinical pneumococcal strains that are bile insoluble","volume":"40","author":"Fenoll","year":"2002","journal-title":"J. Clin. Microbiol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"4686","DOI":"10.1128\/JCM.42.10.4686-4696.2004","article-title":"Accuracy of phenotypic and genotypic testing for identification of Streptococcus pneumoniae and description of Streptococcus pseudopneumoniae sp. nov","volume":"42","author":"Arbique","year":"2004","journal-title":"J. Clin. Microbiol."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1128\/JCM.44.4.1250-1256.2006","article-title":"Characteristic signatures of the lytA gene provide a rapid and reliable diagnosis of Streptococcus pneumoniae infections","volume":"44","author":"Llull","year":"2006","journal-title":"J. Clin. Microbiol."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"1020","DOI":"10.1038\/nsb724","article-title":"A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA","volume":"8","author":"Romero","year":"2001","journal-title":"Nat. Struct. Biol."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/S0022-2836(02)00596-X","article-title":"Two new crystal forms of the choline-binding domain of the major pneumococcal autolysin: Insights into the dynamics of the active homodimer","volume":"321","author":"Romero","year":"2002","journal-title":"J. Mol. Biol."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"e01120-13","DOI":"10.1128\/mBio.01120-13","article-title":"Structural and functional insights into peptidoglycan access for the lytic amidase LytA of Streptococcus pneumoniae","volume":"5","author":"Mellroth","year":"2014","journal-title":"mBio"},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"1373","DOI":"10.1107\/S1399004715007403","article-title":"Full-length structure of the major autolysin LytA","volume":"71","author":"Li","year":"2015","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1038\/nsmb940","article-title":"Insights into pneumococcal pathogenesis from the crystal structure of the modular teichoic acid phosphorylcholine esterase Pce","volume":"12","author":"Hermoso","year":"2005","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"3347","DOI":"10.1074\/jbc.REV119.010155","article-title":"Uncovering the activities, biological roles, and regulation of bacterial cell wall hydrolases and tailoring enzymes","volume":"295","author":"Do","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref_193","doi-asserted-by":"crossref","unstructured":"Brogan, A.P., and Rudner, D.Z. (2023). Regulation of peptidoglycan hydrolases: Localization, abundance, and activity. Curr. Opin. Microbiol., 72.","DOI":"10.1016\/j.mib.2023.102279"},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1016\/j.femsre.2004.05.002","article-title":"Recent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophage","volume":"28","year":"2004","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"1238","DOI":"10.1016\/S0021-9258(19)85077-9","article-title":"Subcellular localization of the major pneumococcal autolysin: A peculiar mechanism of secretion in Escherichia coli","volume":"264","author":"Ascaso","year":"1989","journal-title":"J. Biol. Chem."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"8076","DOI":"10.1002\/chem.201500447","article-title":"Micelle-triggered \u03b2-hairpin to \u03b1-helix transition in a 14-residue peptide from a choline-binding repeat of the pneumococcal autolysin LytA","volume":"21","author":"Maestro","year":"2015","journal-title":"Chemistry"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"5825","DOI":"10.1002\/chem.201704802","article-title":"Roles of amphipathicity and hydrophobicity in the micelle-driven structural switch of a 14-mer peptide core from a choline-binding repeat","volume":"24","author":"Maestro","year":"2018","journal-title":"Chem. Eur. J."},{"key":"ref_198","doi-asserted-by":"crossref","unstructured":"Gomez, M.V., Ruiz-Casta\u00f1eda, M., Nitschke, P., Gschwind, R.M., and Jim\u00e9nez, M.A. (2021). Insights Into the micelle-induced \u03b2-hairpin-to-\u03b1-helix transition of a LytA-derived peptide by photo-CIDNP spectroscopy. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22136666"},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"2971","DOI":"10.1021\/acs.biochem.7b00375","article-title":"Metamorphic proteins: Emergence of dual protein folds from one primary sequence","volume":"56","author":"Lella","year":"2017","journal-title":"Biochemistry"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1002\/cbic.201900446","article-title":"Turncoat polypeptides: We adapt to our environment","volume":"21","author":"Maestro","year":"2020","journal-title":"Chembiochem"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"38506","DOI":"10.1021\/acsomega.4c03658","article-title":"Chameleon sequences-Structural effects in proteins characterized by hydrophobicity disorder","volume":"9","author":"Roterman","year":"2024","journal-title":"ACS Omega"},{"key":"ref_202","doi-asserted-by":"crossref","unstructured":"Porter, L.L., Artsimovitch, I., and Ram\u00edrez-Sarmiento, C.A. (2024). Metamorphic proteins and how to find them. Curr. Opin. Struct. Biol., 86.","DOI":"10.1016\/j.sbi.2024.102807"},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1007\/s12275-015-5432-6","article-title":"Stress responses in Streptococcus species and their effects on the host","volume":"53","author":"Nguyen","year":"2015","journal-title":"J. Microbiol."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1128\/MMBR.00076-15","article-title":"Stress physiology of lactic acid bacteria","volume":"80","author":"Papadimitriou","year":"2016","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"e02456-20","DOI":"10.1128\/mBio.02456-20","article-title":"Bacterial cell wall quality control during environmental stress","volume":"11","author":"Mueller","year":"2020","journal-title":"mBio"},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1055\/s-2000-9138","article-title":"Temperatur- und feuchteprofil der nasenwege vor und nach schleimhautabschwellung durch xylometazolin","volume":"79","author":"Keck","year":"2000","journal-title":"Laryngorhinootologie"},{"key":"ref_207","doi-asserted-by":"crossref","unstructured":"Abbas, A.K., Heimann, K., Jergus, K., Orlikowsky, T., and Leonhardt, S. (2011). Neonatal non-contact respiratory monitoring based on real-time infrared thermography. Biomed. Eng. Online, 10.","DOI":"10.1186\/1475-925X-10-93"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"e0040021","DOI":"10.1128\/IAI.00400-21","article-title":"Glutamate dehydrogenase (GdhA) of Streptococcus pneumoniae is required for high temperature adaptation","volume":"89","author":"Gazioglu","year":"2021","journal-title":"Infect. Immun."},{"key":"ref_209","doi-asserted-by":"crossref","unstructured":"Sakai, F., Talekar, S.J., Lanata, C.F., Grijalva, C.G., Klugman, K.P., Vidal, J.E., and for the RESPIRA PERU Group (2013). Expression of virulence-related genes in the nasopharynx of healthy children. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0067147"},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1016\/j.jaci.2016.04.062","article-title":"Airborne dust and high temperatures are risk factors for invasive bacterial disease","volume":"139","author":"Jusot","year":"2017","journal-title":"J. Allergy Clin. Immunol."},{"key":"ref_211","doi-asserted-by":"crossref","unstructured":"Maziero, M., Lane, D., Polard, P., and Berg\u00e9, M. (2023). Fever-like temperature bursts promote competence development via an HtrA-dependent pathway in Streptococcus pneumoniae. PLoS Genet., 19.","DOI":"10.1101\/2023.04.15.536848"},{"key":"ref_212","doi-asserted-by":"crossref","unstructured":"Ali, M.Q., Kohler, T.P., Schulig, L., Burchhardt, G., and Hammerschmidt, S. (2021). Pneumococcal extracellular serine proteases: Molecular analysis and impact on colonization and disease. Front. Cell. Infect. Microbiol., 11.","DOI":"10.3389\/fcimb.2021.763152"},{"key":"ref_213","doi-asserted-by":"crossref","unstructured":"Eichner, H., Karlsson, J., Spelmink, L., Pathak, A., Sham, L.-T., Henriques-Normark, B., and Loh, E. (2021). RNA thermosensors facilitate Streptococcus pneumoniae and Haemophilus influenzae immune evasion. PLoS Pathog., 17.","DOI":"10.1371\/journal.ppat.1009513"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"1417","DOI":"10.1016\/j.ijporl.2009.07.007","article-title":"Interaction of phase variation, host and pressure\/gas composition: Pneumococcal gene expression of PsaA, SpxB, Ply and LytA in simulated middle ear environments","volume":"73","author":"Lo","year":"2009","journal-title":"Int. J. Pediatr. Otorhinolaryngol."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"5625","DOI":"10.1038\/s41467-024-49853-2","article-title":"Pneumococcal competence is a populational health sensor driving multilevel heterogeneity in response to antibiotics","volume":"15","author":"Prudhomme","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_216","doi-asserted-by":"crossref","unstructured":"Zhang, Y., Guo, S., Li, Y., Zhou, L., and Wu, Y. (2024). Competence regulation in Streptococcus pneumoniae and the competence-targeted anti-pneumococcal strategies. Curr. Med. Chem.","DOI":"10.2174\/0109298673319344240826100841"},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1038\/nrmicro.2017.66","article-title":"Interbacterial predation as a strategy for DNA acquisition in naturally competent bacteria","volume":"15","author":"Veening","year":"2017","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1146\/annurev.micro.60.080805.142139","article-title":"Induction of competence regulons as a general response to stress in Gram-positive bacteria","volume":"60","author":"Claverys","year":"2006","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"3475","DOI":"10.1111\/j.1558-5646.2011.01402.x","article-title":"Competence increases survival during stress in Streptococcus pneumoniae","volume":"65","author":"Engelmoer","year":"2011","journal-title":"Evolution"},{"key":"ref_220","first-page":"e03142-24","article-title":"Competence induction of homologous recombination genes protects pneumococcal cells from genotoxic stress","volume":"16","author":"Soulet","year":"2024","journal-title":"mBio"},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1126\/science.1188308","article-title":"Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells","volume":"329","author":"Taniguchi","year":"2010","journal-title":"Science"},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"2261","DOI":"10.1021\/pr201052x","article-title":"Comparative analysis of different label-free mass spectrometry based protein abundance estimates and their correlation with RNA-Seq gene expression data","volume":"11","author":"Ning","year":"2012","journal-title":"J. Proteome Res."},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1111\/j.1365-2958.2003.03892.x","article-title":"Interconnection of competence, stress and CiaR regulons in Streptococcus pneumoniae: Competence triggers stationary phase autolysis of ciaR mutant cells","volume":"51","author":"Dagkessamanskaia","year":"2004","journal-title":"Mol. Microbiol."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1046\/j.1365-2958.2003.03907.x","article-title":"Identification of competence pheromone responsive genes in Streptococcus pneumoniae by use of DNA microarrays","volume":"51","author":"Peterson","year":"2004","journal-title":"Mol. Microbiol."},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1073\/pnas.55.1.58","article-title":"On the nature of the pneumococcal activator substance","volume":"55","author":"Tomasz","year":"1966","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"11140","DOI":"10.1073\/pnas.92.24.11140","article-title":"An unmodified heptadecapeptide pheromone induces competence for genetic transformation in Streptococcus pneumoniae","volume":"92","author":"Coomaraswamy","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_227","first-page":"9990","article-title":"High-resolution analysis of the pneumococcal transcriptome under a wide range of infection-relevant conditions","volume":"46","author":"Aprianto","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"ref_228","doi-asserted-by":"crossref","unstructured":"Aprianto, R., Slager, J., Holsappel, S., and Veening, J.-W. (2016). Time-resolved dual RNA-seq reveals extensive rewiring of lung epithelial and pneumococcal transcriptomes during early infection. Genome Biol., 17.","DOI":"10.1186\/s13059-016-1054-5"},{"key":"ref_229","doi-asserted-by":"crossref","unstructured":"Minhas, V., Domenech, A., Synefiaridou, D., Straume, D., Brendel, M., Cebrero, G., Liu, X., Costa, C., Baldry, M., and Sirard, J.-C. (2023). Competence remodels the pneumococcal cell wall exposing key surface virulence factors that mediate increased host adherence. PLoS Biol., 21.","DOI":"10.1371\/journal.pbio.3001990"},{"key":"ref_230","doi-asserted-by":"crossref","unstructured":"Lavergne, J.-P., Page, A., Polard, P., Campo, N., and Grangeasse, C. (2025). Quantitative phosphoproteomic reveals that the induction of competence modulates protein phosphorylation in Streptococcus pneumonaie. J. Proteom., 105399.","DOI":"10.1016\/j.jprot.2025.105399"},{"key":"ref_231","doi-asserted-by":"crossref","unstructured":"Zhu, L., and Lau, G.W. (2011). Inhibition of competence development, horizontal gene transfer and virulence in Streptococcus pneumoniae by a modified competence stimulating peptide. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1002241"},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1111\/j.1365-2958.2009.06789.x","article-title":"SpxA1, a novel transcriptional regulator involved in X-state (competence) development in Streptococcus pneumoniae","volume":"73","author":"Turlan","year":"2009","journal-title":"Mol. Microbiol."},{"key":"ref_233","doi-asserted-by":"crossref","unstructured":"Wang, S., Li, X.-Y., Zhu, M., Deng, H., Wang, J., and Zhang, J.-R. (2024). The SpxA1-TenA toxin-antitoxin system regulates epigenetic variations of Streptococcus pneumoniae by targeting protein synthesis. PLoS Pathog., 20.","DOI":"10.1371\/journal.ppat.1012801"},{"key":"ref_234","doi-asserted-by":"crossref","unstructured":"Chan, W.T., Garcill\u00e1n-Barcia, M.P., Yeo, C.C., and Espinosa, M. (2023). Type II bacterial toxin\u2013antitoxins: Hypotheses, facts, and the newfound plethora of the PezAT system. FEMS Microbiol. Rev., 47.","DOI":"10.1093\/femsre\/fuad052"},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"e00919-19","DOI":"10.1128\/IAI.00919-19","article-title":"Streptococcus pneumoniae elaborates persistent and prolonged competent state during pneumonia-derived sepsis","volume":"88","author":"Lin","year":"2020","journal-title":"Infect. Immun."},{"key":"ref_236","doi-asserted-by":"crossref","unstructured":"Chong, S.Y., Lew, S.Q., Alam, T., Gaulke, C.A., and Lau, G.W. (2025). Comparative analysis of the Streptococcus pneumoniae competence development in vitro versus in vivo during pneumonia-derived sepsis. Front. Microbiol., 16.","DOI":"10.3389\/fmicb.2025.1540511"},{"key":"ref_237","doi-asserted-by":"crossref","unstructured":"Schmidt, F., Kakar, N., Meyer, T.C., Depke, M., Masouris, I., Burchhardt, G., G\u00f3mez-Mejia, A., Dhople, V., H\u00e5varstein, L.S., and Sun, Z. (2019). In vivo proteomics identifies the competence regulon and AliB oligopeptide transporter as pathogenic factors in pneumococcal meningitis. PLoS Pathog., 15.","DOI":"10.1371\/journal.ppat.1007987"},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"111851","DOI":"10.1016\/j.celrep.2022.111851","article-title":"Pneumolysin promotes host cell necroptosis and bacterial competence during pneumococcal meningitis as shown by whole-animal dual RNA-seq","volume":"41","author":"Jim","year":"2022","journal-title":"Cell Rep."},{"key":"ref_239","doi-asserted-by":"crossref","unstructured":"Shenoy, A.T., Brissac, T., Gilley, R.P., Kumar, N., Wang, Y., Gonzalez-Juarbe, N., Hinkle, W.S., Daugherty, S.C., Shetty, A.C., and Ott, S. (2017). Streptococcus pneumoniae in the heart subvert the host response through biofilm-mediated resident macrophage killing. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006582"},{"key":"ref_240","doi-asserted-by":"crossref","unstructured":"Shenoy, A.T., Beno, S.M., Brissac, T., Bell, J.W., Novak, L., and Orihuela, C.J. (2018). Severity and properties of cardiac damage caused by Streptococcus pneumoniae are strain dependent. PLoS ONE, 13.","DOI":"10.1371\/journal.pone.0204032"},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"33507","DOI":"10.1073\/pnas.2010428117","article-title":"An in vivo atlas of host\u2013pathogen transcriptomes during Streptococcus pneumoniae colonization and disease","volume":"117","author":"Riegler","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"5582","DOI":"10.1128\/IAI.72.10.5582-5596.2004","article-title":"Microarray analysis of pneumococcal gene expression during invasive disease","volume":"72","author":"Orihuela","year":"2004","journal-title":"Infect. Immun."},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1099\/mic.0.28406-0","article-title":"LuxS impacts on LytA-dependent autolysis and on competence in Streptococcus pneumoniae","volume":"152","author":"Romao","year":"2006","journal-title":"Microbiology"},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1093\/jac\/dkl560","article-title":"Gene expression profiling of the response of Streptococcus pneumoniae to penicillin","volume":"59","author":"Rogers","year":"2007","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_245","doi-asserted-by":"crossref","unstructured":"Yadav, M.K., Vidal, J.E., Go, Y.Y., Kim, S.H., Chae, S.-W., and Song, J.-J. (2018). The LuxS\/AI-2 quorum-sensing system of Streptococcus pneumoniae is required to cause disease, and to regulate virulence- and metabolism-related genes in a rat model of middle ear infection. Front. Cell. Infect. Microbiol., 8.","DOI":"10.3389\/fcimb.2018.00138"},{"key":"ref_246","doi-asserted-by":"crossref","first-page":"4050","DOI":"10.1128\/IAI.05186-11","article-title":"The LuxS-dependent quorum-sensing system regulates early biofilm formation by Streptococcus pneumoniae strain D39","volume":"79","author":"Vidal","year":"2011","journal-title":"Infect. Immun."},{"key":"ref_247","doi-asserted-by":"crossref","unstructured":"Yadav, M.K., Go, Y.Y., Chae, S.W., Park, M.K., and Song, J.J. (2020). Asian sand dust particles increased pneumococcal biofilm formation in vitro and colonization in human middle ear epithelial cells and rat middle ear mucosa. Front. Genet., 11.","DOI":"10.3389\/fgene.2020.00323"},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"e02125-19","DOI":"10.1128\/AEM.02125-19","article-title":"Electronic Cigarette (E-cigarette) vapor exposure alters Streptococcus pneumoniae transcriptome in a nicotine-dependent manner without affecting pneumococcal virulence","volume":"86","author":"Bagale","year":"2019","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"e00161-18","DOI":"10.1128\/AAC.00161-18","article-title":"Mechanism of macrolide-induced inhibition of pneumolysin release involves impairment of autolysin release in macrolide-resistant Streptococcus pneumoniae","volume":"62","author":"Domon","year":"2018","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_250","doi-asserted-by":"crossref","unstructured":"Domon, H., Isono, T., Hiyoshi, T., Tamura, H., Sasagawa, K., Maekawa, T., Hirayama, S., Yanagihara, K., and Terao, Y. (2021). Clarithromycin inhibits pneumolysin production via downregulation of ply gene transcription despite autolysis activation. Microbiol. Spectr., 9.","DOI":"10.1128\/Spectrum.00318-21"},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/j.micinf.2013.11.006","article-title":"Nontypeable Haemophilus influenzae inhibits autolysis and fratricide of Streptococcus pneumoniae in vitro","volume":"16","author":"Hong","year":"2014","journal-title":"Microbes Infect."},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"e27318","DOI":"10.1002\/ppul.27318","article-title":"Haemophilus influenzae and pneumococci: Co-colonization, interactions, cooperation and competition","volume":"60","author":"McMahon","year":"2024","journal-title":"Pediatr. Pulmonol."},{"key":"ref_253","doi-asserted-by":"crossref","unstructured":"Alvarez, A.F., and Georgellis, D. (2023). Environmental adaptation and diversification of bacterial two-component systems. Curr. Opin. Microbiol., 76.","DOI":"10.1016\/j.mib.2023.102399"},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1016\/j.ijmm.2017.11.012","article-title":"Streptococcus pneumoniae two-component regulatory systems: The interplay of the pneumococcus with its environment","volume":"308","author":"Hammerschmidt","year":"2018","journal-title":"Int. J. Med. Microbiol."},{"key":"ref_255","doi-asserted-by":"crossref","unstructured":"Pettersen, J.S., Nielsen, F.D., Andreassen, P.R., M\u00f8ller-Jensen, J., and J\u00f8rgensen, M.G. (2024). A comprehensive analysis of pneumococcal two-component system regulatory networks. NAR Genom. Bioinform., 6.","DOI":"10.1093\/nargab\/lqae039"},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"1959","DOI":"10.1128\/JB.188.5.1959-1968.2006","article-title":"The CiaRH system of Streptococcus pneumoniae prevents lysis during stress induced by treatment with cell wall inhibitors and by mutations in pbp2x involved in \u03b2-lactam resistance","volume":"188","author":"Mascher","year":"2006","journal-title":"J. Bacteriol."},{"key":"ref_257","first-page":"211","article-title":"The ciaR\/ciaH regulatory network of Streptococcus pneumoniae","volume":"4","author":"Kaminski","year":"2002","journal-title":"J. Mol. Microbiol. Biotechnol."},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1111\/j.1365-2958.2007.05900.x","article-title":"Identification of the genes directly controlled by the response regulator CiaR in Streptococcus pneumoniae: Five out of 15 promoters drive expression of small non-coding RNAs","volume":"66","author":"Halfmann","year":"2007","journal-title":"Mol. Microbiol."},{"key":"ref_259","first-page":"96","article-title":"Activity of the two-component regulatory system CiaRH in Streptococcus pneumoniae R6","volume":"20","author":"Halfmann","year":"2011","journal-title":"J. Mol. Microbiol. Biotechnol."},{"key":"ref_260","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1128\/JB.01204-09","article-title":"Identification and characterization of noncoding small RNAs in Streptococcus pneumoniae serotype 2 strain D39","volume":"192","author":"Tsui","year":"2010","journal-title":"J. Bacteriol."},{"key":"ref_261","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1089\/mdr.1998.4.25","article-title":"Versatility of choline-binding domain","volume":"4","author":"Medrano","year":"1998","journal-title":"Microb. Drug Resist."},{"key":"ref_262","unstructured":"Rodr\u00edguez S\u00e1nchez-Beato, A.I. (2005). Caracterizaci\u00f3n Molecular de Genes de Clostridium acetobutylicum y Streptococcus pneumoniae que codifican Para Prote\u00ednas con Dominios de Uni\u00f3n a Colina. [Ph.D. Thesis, Universidad Complutense de Madrid]. Available online: https:\/\/docta.ucm.es\/bitstreams\/274074c1-1c65-4064-a70c-d34c568eb827\/download."},{"key":"ref_263","doi-asserted-by":"crossref","first-page":"1761","DOI":"10.1128\/JB.01489-09","article-title":"The pneumococcal cell envelope stress-sensing system LiaFSR is activated by murein hydrolases and lipid II-interacting antibiotics","volume":"192","author":"Eldholm","year":"2010","journal-title":"J. Bacteriol."},{"key":"ref_264","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1038\/embor.2008.245","article-title":"Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae","volume":"10","author":"Molina","year":"2009","journal-title":"EMBO Rep."},{"key":"ref_265","doi-asserted-by":"crossref","first-page":"4405","DOI":"10.1128\/IAI.71.8.4405-4413.2003","article-title":"Contribution of a response regulator to the virulence of Streptococcus pneumoniae is strain dependent","volume":"71","author":"Blue","year":"2003","journal-title":"Infect. Immun."},{"key":"ref_266","doi-asserted-by":"crossref","unstructured":"Hirschmann, S., G\u00f3mez-Mejia, A., M\u00e4der, U., Karsunke, J., Driesch, D., Rohde, M., H\u00e4ussler, S., Burchhardt, G., and Hammerschmidt, S. (2021). The two-component system 09 regulates pneumococcal carbohydrate metabolism and capsule expression. Microorganisms, 9.","DOI":"10.3390\/microorganisms9030468"},{"key":"ref_267","doi-asserted-by":"crossref","unstructured":"Hirschmann, S., G\u00f3mez-Mejia, A., Kohler, T.P., Vo\u00df, F., Rohde, M., Brendel, M., and Hammerschmidt, S. (2021). The two-component system 09 of Streptococcus pneumoniae is important for metabolic fitness and resistance during dissemination in the host. Microorganisms, 9.","DOI":"10.3390\/microorganisms9071365"},{"key":"ref_268","first-page":"935","article-title":"Inhibition of autolysis by lipase LipA in Streptococcus pneumoniae sepsis","volume":"40","author":"Kim","year":"2017","journal-title":"Mol. Cells"},{"key":"ref_269","doi-asserted-by":"crossref","first-page":"5797","DOI":"10.1128\/JB.00336-06","article-title":"A functional dlt operon, encoding proteins required for incorporation of d-alanine in teichoic acids in Gram-positive bacteria, confers resistance to cationic antimicrobial peptides in Streptococcus pneumoniae","volume":"188","author":"Halfmann","year":"2006","journal-title":"J. Bacteriol."},{"key":"ref_270","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1089\/mdr.1996.2.123","article-title":"d-Alanine deprivation of Bacillus subtilis teichoic acids is without effect on cell growth and morphology but affects the autolytic activity","volume":"2","author":"Wecke","year":"1996","journal-title":"Microb. Drug Resist."},{"key":"ref_271","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1128\/JB.187.1.114-124.2005","article-title":"Autolysis of Lactococcus lactis is increased upon d-alanine depletion of peptidoglycan and lipoteichoic acids","volume":"187","author":"Steen","year":"2005","journal-title":"J. Bacteriol."},{"key":"ref_272","doi-asserted-by":"crossref","first-page":"225","DOI":"10.2217\/fmb-2022-0165","article-title":"Dlt operon regulates physiological function and cariogenic virulence in Streptococcus mutans","volume":"18","author":"Du","year":"2023","journal-title":"Future Microbiol."},{"key":"ref_273","doi-asserted-by":"crossref","first-page":"3556","DOI":"10.1128\/JB.01981-14","article-title":"Spermidine biosynthesis and transport modulate pneumococcal autolysis","volume":"196","author":"Potter","year":"2014","journal-title":"J. Bacteriol."},{"key":"ref_274","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1038\/s41579-019-0196-3","article-title":"Definitions and guidelines for research on antibiotic persistence","volume":"17","author":"Balaban","year":"2019","journal-title":"Nat. Rev. Microbiol"},{"key":"ref_275","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1111\/nyas.14541","article-title":"Understanding tolerance to cell wall-active antibiotics","volume":"1496","year":"2021","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_276","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1038\/nrmicro.2016.34","article-title":"Distinguishing between resistance, tolerance and persistence to antibiotic treatment","volume":"14","author":"Brauner","year":"2016","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_277","doi-asserted-by":"crossref","unstructured":"Wan, Y., Zheng, J., Chan, E.W., and Chen, S. (2024). Proton motive force and antibiotic tolerance in bacteria. Microb. Biotechnol., 17.","DOI":"10.1111\/1751-7915.70042"},{"key":"ref_278","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1038\/s41579-022-00820-y","article-title":"Molecular mechanisms of antibiotic resistance revisited","volume":"21","author":"Darby","year":"2023","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_279","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/bs.ampbs.2023.04.002","article-title":"Bacterial metabolism and susceptibility to cell wall-active antibiotics","volume":"83","author":"Keller","year":"2023","journal-title":"Adv. Microb. Physiol."},{"key":"ref_280","doi-asserted-by":"crossref","first-page":"e02828-23","DOI":"10.1128\/mbio.02828-23","article-title":"Streptococcus pneumoniae favors tolerance via metabolic adaptation over resistance to circumvent fluoroquinolones","volume":"15","author":"Dao","year":"2024","journal-title":"mBio"},{"key":"ref_281","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1128\/AAC.10.4.697","article-title":"Suppression of the lytic and bactericidal effects of cell wall-inhibitory antibiotics","volume":"10","author":"Lopez","year":"1976","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_282","doi-asserted-by":"crossref","first-page":"3293","DOI":"10.1073\/pnas.73.9.3293","article-title":"Suppression of lytic effect of beta lactams on Escherichia coli and other bacteria","volume":"73","author":"Goodell","year":"1976","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_283","doi-asserted-by":"crossref","unstructured":"Ataee, R.A., Habibian, S., Mehrabi-Tavana, A., Ahmadi, Z., Jonaidi, N., and Salesi, M. (2014). Determination of vancomycin minimum inhibitory concentration for ceftazidime resistant Streptococcus pneumoniae in Iran. Ann. Clin. Microbiol. Antimicrob., 13.","DOI":"10.1186\/s12941-014-0053-1"},{"key":"ref_284","first-page":"e57285","article-title":"Characterization of 5 episodes of vancomycin nonsusceptible Streptococcus pneumoniae from clinical isolates in Tehran, Iran","volume":"12","author":"Hashemi","year":"2017","journal-title":"Arch. Clin. Infect. Dis."},{"key":"ref_285","unstructured":"The European Committee on Antimicrobial Susceptibility Testing (EUCAST) (2025, March 05). Breakpoint Tables for Interpretation of MICs and Zone Diameters. Version 14.0. Available online: https:\/\/www.eucast.org\/fileadmin\/src\/media\/PDFs\/EUCAST_files\/Breakpoint_tables\/v_14.0_Breakpoint_Tables.pdf."},{"key":"ref_286","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/S0924-8579(99)00113-2","article-title":"Vancomycin resistance in Gram-positive bacteria other than Enterococcus spp","volume":"14","author":"Sefton","year":"2000","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_287","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1093\/infdis\/jiae393","article-title":"The emergent invasive serotype 4 ST10172 strain acquires vanG-type vancomycin-resistance element: A case of a 66-year-old with bacteremic pneumococcal pneumonia","volume":"231","author":"Chochua","year":"2024","journal-title":"J. Infect. Dis."},{"key":"ref_288","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1111\/j.1758-2229.2011.00254.x","article-title":"Vancomycin tolerance in Gram-positive cocci","volume":"3","author":"Moscoso","year":"2011","journal-title":"Environ. Microbiol. Rep."},{"key":"ref_289","doi-asserted-by":"crossref","unstructured":"Li, G., Walker, M.J., and De Oliveira, D.M.P. (2022). Vancomycin resistance in Enterococcus and Staphylococcus aureus. Microorganisms, 11.","DOI":"10.3390\/microorganisms11010024"},{"key":"ref_290","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1046\/j.1469-0691.2002.00477.x","article-title":"Antibiotic tolerance in pneumococci","volume":"8","author":"Normark","year":"2002","journal-title":"Clin. Microbiol. Infect."},{"key":"ref_291","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1078\/1438-4221-00193","article-title":"Molecular analysis of antibiotic tolerance in pneumococci","volume":"292","author":"Mitchell","year":"2002","journal-title":"Int. J. Med. Microbiol."},{"key":"ref_292","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1126\/science.aaj2191","article-title":"Antibiotic tolerance facilitates the evolution of resistance","volume":"355","author":"Ronin","year":"2017","journal-title":"Science"},{"key":"ref_293","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1126\/science.aay3041","article-title":"Effect of tolerance on the evolution of antibiotic resistance under drug combinations","volume":"367","author":"Liu","year":"2020","journal-title":"Science"},{"key":"ref_294","doi-asserted-by":"crossref","first-page":"2776","DOI":"10.1128\/IAI.67.6.2776-2782.1999","article-title":"Molecular characterization of equine isolates of Streptococcus pneumoniae: Natural disruption of genes encoding the virulence factors pneumolysin and autolysin","volume":"67","author":"Whatmore","year":"1999","journal-title":"Infect. Immun."},{"key":"ref_295","doi-asserted-by":"crossref","unstructured":"Wong, H.E., Tourlomousis, P., Paterson, G.K., Webster, S., and Bryant, C.E. (2023). Naturally-occurring serotype 3 Streptococcus pneumoniae strains that lack functional pneumolysin and autolysin have attenuated virulence but induce localized protective immune responses. PLoS ONE, 18.","DOI":"10.1371\/journal.pone.0282843"},{"key":"ref_296","doi-asserted-by":"crossref","first-page":"3524","DOI":"10.1128\/JCM.00558-06","article-title":"Vancomycin-tolerant Streptococcus pneumoniae in Korea","volume":"44","author":"Sung","year":"2006","journal-title":"J. Clin. Microbiol."},{"key":"ref_297","doi-asserted-by":"crossref","first-page":"1052","DOI":"10.1111\/j.1365-2958.2010.07271.x","article-title":"Vancomycin tolerance in clinical and laboratory Streptococcus pneumoniae isolates depends on reduced enzyme activity of the major LytA autolysin or cooperation between CiaH histidine kinase and capsular polysaccharide","volume":"77","author":"Moscoso","year":"2010","journal-title":"Mol. Microbiol."},{"key":"ref_298","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1046\/j.1365-2958.1998.01016.x","article-title":"Penicillin tolerance genes of Streptococcus pneumoniae: The ABC-type manganese permease complex Psa","volume":"29","author":"Novak","year":"1998","journal-title":"Mol. Microbiol."},{"key":"ref_299","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1046\/j.1365-2958.2000.01854.x","article-title":"Extracellular targeting of choline-binding proteins in Streptococcus pneumoniae by a zinc metalloprotease","volume":"36","author":"Novak","year":"2000","journal-title":"Mol. Microbiol."},{"key":"ref_300","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1046\/j.1365-2958.1999.01369.x","article-title":"Penicillin tolerance in Streptococcus pneumoniae, autolysis and the Psa ATP-binding cassette (ABC) manganese permease","volume":"32","author":"Claverys","year":"1999","journal-title":"Mol. Microbiol."},{"key":"ref_301","doi-asserted-by":"crossref","first-page":"1651","DOI":"10.1046\/j.1365-2958.2001.02359.x","article-title":"The puzzle of zmpB and extensive chain formation, autolysis defect and non-translocation of choline-binding proteins in Streptococcus pneumoniae","volume":"39","author":"Iannelli","year":"2001","journal-title":"Mol. Microbiol."},{"key":"ref_302","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1111\/j.1365-2958.2004.04164.x","article-title":"Molecular analysis of the psa permease complex of Streptococcus pneumoniae","volume":"53","author":"McAllister","year":"2004","journal-title":"Mol. Microbiol."},{"key":"ref_303","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1046\/j.1365-2958.2000.02011.x","article-title":"Regulation of growth inhibition at high temperature, autolysis, transformation and adherence in Streptococcus pneumoniae by ClpC","volume":"37","author":"Charpentier","year":"2000","journal-title":"Mol. Microbiol."},{"key":"ref_304","doi-asserted-by":"crossref","first-page":"730","DOI":"10.1128\/IAI.73.2.730-740.2005","article-title":"Contribution of the ATP-dependent protease ClpCP to the autolysis and virulence of Streptococcus pneumoniae","volume":"73","author":"Ibrahim","year":"2005","journal-title":"Infect. Immun."},{"key":"ref_305","doi-asserted-by":"crossref","first-page":"7295","DOI":"10.1128\/JB.183.24.7295-7307.2001","article-title":"Regulation of Streptococcus pneumoniae clp genes and their role in competence development and stress survival","volume":"183","author":"Chastanet","year":"2001","journal-title":"J. Bacteriol."},{"key":"ref_306","doi-asserted-by":"crossref","first-page":"3508","DOI":"10.1128\/JB.184.13.3508-3520.2002","article-title":"Global transcriptional analysis of clpP mutations of type 2 Streptococcus pneumoniae and their effects on physiology and virulence","volume":"184","author":"Robertson","year":"2002","journal-title":"J. Bacteriol."},{"key":"ref_307","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/S1097-2765(00)80402-5","article-title":"Signal transduction by a death signal peptide: Uncovering the mechanism of bacterial killing by penicillin","volume":"5","author":"Novak","year":"2000","journal-title":"Mol. Cell"},{"key":"ref_308","doi-asserted-by":"crossref","first-page":"6987","DOI":"10.1128\/JB.184.24.6987-7000.2002","article-title":"Vancomycin tolerance induced by erythromycin but not by loss of vncRS, vex3, or pep27 function in Streptococcus pneumoniae","volume":"184","author":"Robertson","year":"2002","journal-title":"J. Bacteriol."},{"key":"ref_309","doi-asserted-by":"crossref","first-page":"8463","DOI":"10.1128\/JB.186.24.8463-8471.2004","article-title":"Revising the role of the pneumococcal vex-vncRS locus in vancomycin tolerance","volume":"186","author":"Haas","year":"2004","journal-title":"J. Bacteriol."},{"key":"ref_310","doi-asserted-by":"crossref","first-page":"8205","DOI":"10.1128\/JB.187.23.8205-8210.2005","article-title":"Vancomycin stress response in a sensitive and a tolerant strain of Streptococcus pneumoniae","volume":"187","author":"Haas","year":"2005","journal-title":"J. Bacteriol."},{"key":"ref_311","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1089\/omi.2017.0098","article-title":"Comparative proteomics of Streptococcus pneumoniae response to vancomycin treatment","volume":"21","author":"Yang","year":"2017","journal-title":"OMICS"},{"key":"ref_312","doi-asserted-by":"crossref","first-page":"e00054-17","DOI":"10.1128\/JB.00054-17","article-title":"Transcriptional repressor PtvR regulates phenotypic tolerance to vancomycin in Streptococcus pneumoniae","volume":"199","author":"Liu","year":"2017","journal-title":"J. Bacteriol."},{"key":"ref_313","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1093\/infdis\/157.6.1150","article-title":"Penicillin resistance and defective lysis in clinical isolates of pneumococci: Evidence for two kinds of antibiotic pressure operating in the clinical environment","volume":"157","author":"Moreillon","year":"1988","journal-title":"J. Infect. Dis."},{"key":"ref_314","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1128\/AAC.34.1.33","article-title":"Two bactericidal targets for penicillin in pneumococci: Autolysis-dependent and autolysis-independent killing mechanisms","volume":"34","author":"Moreillon","year":"1990","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_315","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1089\/10766290152773310","article-title":"The role of murMN operon in penicillin resistance and antibiotic tolerance of Streptococcus pneumoniae","volume":"7","author":"Filipe","year":"2001","journal-title":"Microb. Drug Resist."},{"key":"ref_316","doi-asserted-by":"crossref","first-page":"1550","DOI":"10.1073\/pnas.032671699","article-title":"The murMN operon: A functional link between antibiotic resistance and antibiotic tolerance in Streptococcus pneumoniae","volume":"99","author":"Filipe","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_317","doi-asserted-by":"crossref","first-page":"e2018089118","DOI":"10.1073\/pnas.2018089118","article-title":"A molecular link between cell wall biosynthesis, translation fidelity, and stringent response in Streptococcus pneumoniae","volume":"118","author":"Aggarwal","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_318","doi-asserted-by":"crossref","first-page":"1497","DOI":"10.1111\/j.1365-2958.2006.05340.x","article-title":"Attenuation of penicillin resistance in a peptidoglycan O-acetyl transferase mutant of Streptococcus pneumoniae","volume":"61","author":"Vollmer","year":"2006","journal-title":"Mol. Microbiol."},{"key":"ref_319","doi-asserted-by":"crossref","first-page":"832","DOI":"10.1111\/mmi.13849","article-title":"Peptidoglycan O-acetylation is functionally related to cell wall biosynthesis and cell division in Streptococcus pneumoniae","volume":"106","author":"Bonnet","year":"2017","journal-title":"Mol. Microbiol."},{"key":"ref_320","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1086\/380564","article-title":"Capsular expression in Streptococcus pneumoniae negatively affects spontaneous and antibiotic-induced lysis and contributes to antibiotic tolerance","volume":"189","author":"Fernebro","year":"2004","journal-title":"J. Infect. Dis."},{"key":"ref_321","doi-asserted-by":"crossref","unstructured":"Figueiredo, J., Henriques, M.X., Catal\u00e3o, M.J., Pinheiro, S., Narciso, A.R., Mesquita, F., Saraiva, B.M., Carido, M., Cabanes, D., and Pinho, M.G. (2022). Encapsulation of the septal cell wall protects Streptococcus pneumoniae from its major peptidoglycan hydrolase and host defenses. PLoS Pathog., 18.","DOI":"10.1371\/journal.ppat.1010516"},{"key":"ref_322","doi-asserted-by":"crossref","unstructured":"Ghosh, P., Shah, M., Ravichandran, S., Park, S.-S., Iqbal, H., Choi, S., Kim, K.K., and Rhee, D.K. (2019). Pneumococcal VncR strain-specifically regulates capsule polysaccharide synthesis. Front. Microbiol., 10.","DOI":"10.3389\/fmicb.2019.02279"},{"key":"ref_323","doi-asserted-by":"crossref","first-page":"179","DOI":"10.14348\/molcells.2021.2235","article-title":"Crystal structure of the pneumococcal vancomycin-resistance response regulator DNA-binding domain","volume":"44","author":"Park","year":"2021","journal-title":"Mol. Cells"},{"key":"ref_324","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1128\/jb.124.2.1023-1027.1975","article-title":"Biological effects of lipoteichoic acids","volume":"124","author":"Holtje","year":"1975","journal-title":"J. Bacteriol."},{"key":"ref_325","doi-asserted-by":"crossref","first-page":"1690","DOI":"10.1073\/pnas.72.5.1690","article-title":"Lipoteichoic acid: A specific inhibitor of autolysin activity in pneumococcus","volume":"72","author":"Tomasz","year":"1975","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_326","doi-asserted-by":"crossref","first-page":"2093","DOI":"10.1038\/s41467-017-01720-z","article-title":"Lipoteichoic acid deficiency permits normal growth but impairs virulence of Streptococcus pneumoniae","volume":"8","author":"Waldow","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_327","doi-asserted-by":"crossref","first-page":"3324","DOI":"10.1128\/JB.01696-14","article-title":"A novel protein RafX is important for common cell wall polysaccharide biosynthesis in Streptococcus pneumoniae: Implications for bacterial virulence","volume":"196","author":"Wu","year":"2014","journal-title":"J. Bacteriol."},{"key":"ref_328","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1128\/AAC.13.2.293","article-title":"Secretion of cell wall polymers into the growth medium of lysis-defective pneumococci during treatment with penicillin and other inhibitors of cell wall synthesis","volume":"13","author":"Waks","year":"1978","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_329","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1128\/AAC.13.2.302","article-title":"Characterization of cell wall polymers secreted into the growth medium of lysis-defective pneumococci during treatment with penicillin and other inhibitors of cell wall synthesis","volume":"13","author":"Hakenbeck","year":"1978","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_330","doi-asserted-by":"crossref","first-page":"1513","DOI":"10.1111\/j.1365-2958.2010.07071.x","article-title":"Expression and maintenance of ComD\u2013ComE, the two-component signal-transduction system that controls competence of Streptococcus pneumoniae","volume":"75","author":"Martin","year":"2010","journal-title":"Mol. Microbiol."},{"key":"ref_331","doi-asserted-by":"crossref","unstructured":"Yao, M., Wang, K., Song, G., Hu, Y., Chen, J., Li, T., Liang, L., Wu, J., Xu, H., and Wang, L. (2024). Transcriptional regulation of TacL-mediated lipoteichoic acids biosynthesis by ComE during competence impacts pneumococcal transformation. Front. Cell. Infect. Microbiol., 14.","DOI":"10.3389\/fcimb.2024.1375312"},{"key":"ref_332","doi-asserted-by":"crossref","first-page":"26842","DOI":"10.1016\/S0021-9258(19)61452-3","article-title":"Do sequence repeats play an equivalent role in the choline-binding module of pneumococcal LytA amidase?","volume":"275","author":"Varea","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_333","doi-asserted-by":"crossref","first-page":"8229","DOI":"10.1128\/JB.186.24.8229-8239.2004","article-title":"Characterization of LytA-like N-acetylmuramoyl-l-alanine amidases from two new Streptococcus mitis bacteriophages provides insights into the properties of the major pneumococcal autolysin","volume":"186","author":"Romero","year":"2004","journal-title":"J. Bacteriol."},{"key":"ref_334","doi-asserted-by":"crossref","unstructured":"Erlendsson, S., and Teilum, K. (2020). Binding revisited-avidity in cellular function and signaling. Front. Mol. Biosci., 7.","DOI":"10.3389\/fmolb.2020.615565"},{"key":"ref_335","doi-asserted-by":"crossref","first-page":"17729","DOI":"10.1074\/jbc.M611795200","article-title":"Key role of amino acid residues in the dimerization and catalytic activation of the autolysin LytA, an important virulence factor in Streptococcus pneumoniae","volume":"282","author":"Romero","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_336","doi-asserted-by":"crossref","first-page":"31714","DOI":"10.1074\/jbc.M111.264366","article-title":"Crystal structures of bacterial peptidoglycan amidase AmpD and an unprecedented activation mechanism","volume":"286","author":"Zhang","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_337","doi-asserted-by":"crossref","first-page":"1275","DOI":"10.1046\/j.1365-2958.1999.01238.x","article-title":"LytB, a novel pneumococcal murein hydrolase essential for cell separation","volume":"31","year":"1999","journal-title":"Mol. Microbiol."},{"key":"ref_338","doi-asserted-by":"crossref","first-page":"4988","DOI":"10.1128\/JB.184.18.4988-5000.2002","article-title":"Purification and polar localization of pneumococcal LytB, a putative endo-\u03b2-N-acetylglucosaminidase: The chain-dispersing murein hydrolase","volume":"184","year":"2002","journal-title":"J. Bacteriol."},{"key":"ref_339","doi-asserted-by":"crossref","unstructured":"Rico-Lastres, P., D\u00edez-Mart\u00ednez, R., Iglesias-Bexiga, M., Bustamante, N., Aldridge, C., Hesek, D., Lee, M., Mobashery, S., Gray, J., and Vollmer, W. (2015). Substrate recognition and catalysis by LytB, a pneumococcal peptidoglycan hydrolase involved in virulence. Sci. Rep., 5.","DOI":"10.1038\/srep16198"},{"key":"ref_340","doi-asserted-by":"crossref","first-page":"112756","DOI":"10.1016\/j.celrep.2023.112756","article-title":"Molecular basis of the final step of cell division in Streptococcus pneumoniae","volume":"42","author":"Freton","year":"2023","journal-title":"Cell Rep."},{"key":"ref_341","doi-asserted-by":"crossref","first-page":"11018","DOI":"10.1074\/jbc.M111.318584","article-title":"LytA, the major autolysin of Streptococcus pneumoniae, requires access to the nascent peptidoglycan","volume":"287","author":"Mellroth","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_342","doi-asserted-by":"crossref","first-page":"10572","DOI":"10.1039\/C7CC05646J","article-title":"Specific and spatial labeling of choline-containing teichoic acids in Streptococcus pneumoniae by click chemistry","volume":"53","author":"Bonnet","year":"2017","journal-title":"Chem. Commun."},{"key":"ref_343","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.tcsw.2018.05.001","article-title":"Nascent teichoic acids insertion into the cell wall directs the localization and activity of the major pneumococcal autolysin LytA","volume":"2","author":"Bonnet","year":"2018","journal-title":"Cell Surf."},{"key":"ref_344","doi-asserted-by":"crossref","first-page":"786","DOI":"10.1083\/jcb.47.3.786","article-title":"Radioautographic evidence for equatorial wall growth in a Gram-positive bacterium. Segregation of choline-3H-labeled teichoic acid","volume":"47","author":"Briles","year":"1970","journal-title":"J. Cell Biol."},{"key":"ref_345","doi-asserted-by":"crossref","first-page":"1581","DOI":"10.1128\/jb.151.3.1581-1590.1982","article-title":"Choline-containing bacteriophage receptors in Streptococcus pneumoniae","volume":"151","author":"Lopez","year":"1982","journal-title":"J. Bacteriol."},{"key":"ref_346","doi-asserted-by":"crossref","first-page":"475","DOI":"10.2174\/1566524013363618","article-title":"Genetic bases and medical relevance of capsular polysaccharide biosynthesis in pathogenic streptococci","volume":"1","author":"Llull","year":"2001","journal-title":"Curr. Mol. Med."},{"key":"ref_347","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1146\/annurev.micro.62.081307.162944","article-title":"Capsules of Streptococcus pneumoniae and other bacteria: Paradigms for polysaccharide biosynthesis and regulation","volume":"65","author":"Yother","year":"2011","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_348","doi-asserted-by":"crossref","unstructured":"Paton, J.C., and Trappetti, C. (2019). Streptococcus pneumoniae capsular polysaccharide. Microbiol. Spectr., 7.","DOI":"10.1128\/microbiolspec.GPP3-0019-2018"},{"key":"ref_349","doi-asserted-by":"crossref","first-page":"4931","DOI":"10.1038\/emboj.2011.358","article-title":"A widespread family of bacterial cell wall assembly proteins","volume":"30","author":"Kawai","year":"2011","journal-title":"EMBO J."},{"key":"ref_350","doi-asserted-by":"crossref","unstructured":"Stefanovi\u0107, C., Hager, F.F., and Sch\u00e4ffer, C. (2021). LytR-CpsA-Psr glycopolymer transferases: Essential bricks in Gram-positive bacterial cell wall assembly. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22020908"},{"key":"ref_351","doi-asserted-by":"crossref","unstructured":"Briggs, N.S., Bruce, K.E., Naskar, S., Winkler, M.E., and Roper, D.I. (2021). The pneumococcal divisome: Dynamic control of Streptococcus pneumoniae cell division. Front. Microbiol., 12.","DOI":"10.3389\/fmicb.2021.737396"},{"key":"ref_352","doi-asserted-by":"crossref","first-page":"3170","DOI":"10.1038\/s41467-023-38904-9","article-title":"The divisome but not the elongasome organizes capsule synthesis in Streptococcus pneumoniae","volume":"14","author":"Nakamoto","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_353","doi-asserted-by":"crossref","first-page":"5859","DOI":"10.1128\/JB.00724-09","article-title":"Pneumococcal LytR, a protein from the LytR-CpsA-Psr family, is essential for normal septum formation in Streptococcus pneumoniae","volume":"191","author":"Johnsborg","year":"2009","journal-title":"J. Bacteriol."},{"key":"ref_354","doi-asserted-by":"crossref","unstructured":"Ye, W., Zhang, J., Shu, Z., Yin, Y., Zhang, X., and Wu, K. (2018). Pneumococcal LytR protein is required for the surface attachment of both capsular polysaccharide and teichoic acids: Essential for pneumococcal virulence. Front. Microbiol., 9.","DOI":"10.3389\/fmicb.2018.01199"},{"key":"ref_355","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1089\/mdr.2011.0232","article-title":"Attachment of capsular polysaccharide to the cell wall in Streptococcus pneumoniae","volume":"18","author":"Eberhardt","year":"2012","journal-title":"Microb. Drug Resist."},{"key":"ref_356","doi-asserted-by":"crossref","unstructured":"Battaje, R.R., Piyush, R., Pratap, V., and Panda, D. (2023). Models versus pathogens: How conserved is the FtsZ in bacteria?. Biosci. Rep., 43.","DOI":"10.1042\/BSR20221664"},{"key":"ref_357","doi-asserted-by":"crossref","unstructured":"Perez, A.J., Villicana, J.B., Tsui, H.-C.T., Danforth, M.L., Benedet, M., Massidda, O., and Winkler, M.E. (2021). FtsZ-ring regulation and cell division are mediated by essential EzrA and accessory proteins ZapA and ZapJ in Streptococcus pneumoniae. Front. Microbiol., 12.","DOI":"10.3389\/fmicb.2021.780864"},{"key":"ref_358","doi-asserted-by":"crossref","first-page":"e76392","DOI":"10.7554\/eLife.76392","article-title":"WhyD tailors surface polymers to prevent premature bacteriolysis and direct cell elongation in Streptococcus pneumoniae","volume":"11","author":"Dobihal","year":"2022","journal-title":"eLife"},{"key":"ref_359","doi-asserted-by":"crossref","unstructured":"van der Linden, M., Al-Lahham, A., Nicklas, W., and Reinert, R.R. (2009). Molecular characterization of pneumococcal isolates from pets and laboratory animals. PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0008286"},{"key":"ref_360","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1128\/jcm.20.6.1028-1030.1984","article-title":"Isolation of Streptococcus pneumoniae type 3 from equine species","volume":"20","author":"Benson","year":"1984","journal-title":"J. Clin. Microbiol."},{"key":"ref_361","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1051\/vetres:2004025","article-title":"The pathogenic equine streptococci","volume":"35","author":"Timoney","year":"2004","journal-title":"Vet. Res."},{"key":"ref_362","doi-asserted-by":"crossref","first-page":"6085","DOI":"10.1128\/JB.00468-07","article-title":"New Streptococcus pneumoniae clones in deceased wild chimpanzees","volume":"189","author":"Chi","year":"2007","journal-title":"J. Bacteriol."},{"key":"ref_363","doi-asserted-by":"crossref","unstructured":"Denapaite, D., and Hakenbeck, R. (2011). A new variant of the capsule 3 cluster occurs in Streptococcus pneumoniae from deceased wild chimpanzees. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0025119"},{"key":"ref_364","doi-asserted-by":"crossref","unstructured":"K\u00f6ndgen, S., Calvignac-Spencer, S., Gr\u00fctzmacher, K., Keil, V., M\u00e4tz-Rensing, K., Nowak, K., Metzger, S., Kiyang, J., L\u00fcbke-Becker, A., and Deschner, T. (2017). Evidence for human Streptococcus pneumoniae in wild and captive chimpanzees: A potential threat to wild populations. Sci. Rep., 7.","DOI":"10.1038\/s41598-017-14769-z"},{"key":"ref_365","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1007\/s10393-017-1306-1","article-title":"Pathogen transmission from humans to great apes is a growing threat to primate conservation","volume":"15","author":"Dunay","year":"2018","journal-title":"Ecohealth"},{"key":"ref_366","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1007\/s10393-018-1319-4","article-title":"Human respiratory syncytial virus and Streptococcus pneumoniae infection in wild bonobos","volume":"15","author":"Keil","year":"2018","journal-title":"Ecohealth"},{"key":"ref_367","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1128\/CMR.00012-08","article-title":"Animal models of Streptococcus pneumoniae disease","volume":"21","author":"Chiavolini","year":"2008","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_368","doi-asserted-by":"crossref","unstructured":"Borsa, N., Di Pasquale, M.D., and Restrepo, M.I. (2019). Animal models of pneumococcal pneumonia. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20174220"},{"key":"ref_369","doi-asserted-by":"crossref","unstructured":"Saralahti, A.K., Harjula, S.-K.E., Rantapero, T., Uusi-M\u00e4kel\u00e4, M.I.E., Kaasinen, M., Junno, M., Piippo, H., Nykter, M., Lohi, O., and Rounioja, S. (2023). Characterization of the innate immune response to Streptococcus pneumoniae infection in zebrafish. PLoS Genet., 19.","DOI":"10.1371\/journal.pgen.1010586"},{"key":"ref_370","doi-asserted-by":"crossref","first-page":"e31862","DOI":"10.1016\/j.heliyon.2024.e31862","article-title":"A review on current advancement in zebrafish models to study chronic inflammatory diseases and their therapeutic targets","volume":"10","author":"Balde","year":"2024","journal-title":"Heliyon"},{"key":"ref_371","doi-asserted-by":"crossref","first-page":"2324","DOI":"10.1128\/iai.57.8.2324-2330.1989","article-title":"Contribution of autolysin to virulence of Streptococcus pneumoniae","volume":"57","author":"Berry","year":"1989","journal-title":"Infect. Immun."},{"key":"ref_372","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/0882-4010(92)90111-Z","article-title":"Effect of insertional inactivation of the genes encoding pneumolysin and autolysin on the virulence of Streptococcus pneumoniae type 3","volume":"12","author":"Berry","year":"1992","journal-title":"Microb. Pathog."},{"key":"ref_373","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1128\/IAI.68.1.133-140.2000","article-title":"Additive attenuation of virulence of Streptococcus pneumoniae by mutation of the genes encoding pneumolysin and other putative pneumococcal virulence proteins","volume":"68","author":"Berry","year":"2000","journal-title":"Infect. Immun."},{"key":"ref_374","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1093\/infdis\/172.1.119","article-title":"The role of pneumolysin and autolysin in the pathology of pneumonia and septicemia in mice infected with a type 2 pneumococcus","volume":"172","author":"Canvin","year":"1995","journal-title":"J. Infect. Dis."},{"key":"ref_375","doi-asserted-by":"crossref","first-page":"3108","DOI":"10.1128\/JB.183.10.3108-3116.2001","article-title":"The autolytic enzyme LytA of Streptococcus pneumoniae is not responsible for releasing pneumolysin","volume":"183","author":"Balachandran","year":"2001","journal-title":"J. Bacteriol."},{"key":"ref_376","doi-asserted-by":"crossref","first-page":"5931","DOI":"10.1128\/jb.170.12.5931-5934.1988","article-title":"Insertional inactivation of the major autolysin gene of Streptococcus pneumoniae","volume":"170","author":"Tomasz","year":"1988","journal-title":"J. Bacteriol."},{"key":"ref_377","doi-asserted-by":"crossref","first-page":"1237","DOI":"10.1128\/iai.65.4.1237-1244.1997","article-title":"Differences in virulence for mice among Streptococcus pneumoniae strains of capsular types 2, 3, 4, 5, and 6 are not attributable to differences in pneumolysin production","volume":"65","author":"Benton","year":"1997","journal-title":"Infect. Immun."},{"key":"ref_378","doi-asserted-by":"crossref","first-page":"5534","DOI":"10.1128\/AAC.01470-12","article-title":"Macrolides and \u03b2-lactam antibiotics enhance C3b deposition on the surface of multidrug-resistant Streptococcus pneumoniae strains by a LytA autolysin-dependent mechanism","volume":"56","author":"Olmedillas","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_379","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1128\/IAI.02811-14","article-title":"Pleiotropic effects of the cell wall amidase LytA on Streptococcus pneumoniae sensitivity to the host immune response","volume":"83","author":"Urzainqui","year":"2015","journal-title":"Infect. Immun."},{"key":"ref_380","doi-asserted-by":"crossref","first-page":"1661","DOI":"10.1086\/424596","article-title":"Tissue-specific contributions of pneumococcal virulence factors to pathogenesis","volume":"190","author":"Orihuela","year":"2004","journal-title":"J. Infect. Dis."},{"key":"ref_381","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1086\/527322","article-title":"Streptococcus pneumoniae deficient in pneumolysin or autolysin has reduced virulence in meningitis","volume":"197","author":"Hirst","year":"2008","journal-title":"J. Infect. Dis."},{"key":"ref_382","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/j.dci.2013.09.009","article-title":"Adult zebrafish model for pneumococcal pathogenesis","volume":"42","author":"Saralahti","year":"2014","journal-title":"Dev. Comp. Immunol."},{"key":"ref_383","doi-asserted-by":"crossref","first-page":"2582","DOI":"10.1128\/iai.62.6.2582-2589.1994","article-title":"Phase variation in pneumococcal opacity: Relationship between colonial morphology and nasopharyngeal colonization","volume":"62","author":"Weiser","year":"1994","journal-title":"Infect. Immun."},{"key":"ref_384","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1097\/00006982-200210000-00014","article-title":"Contribution of pneumolysin and autolysin to the pathogenesis of experimental pneumococcal endophthalmitis","volume":"22","author":"Ng","year":"2002","journal-title":"Retina"},{"key":"ref_385","doi-asserted-by":"crossref","unstructured":"Andre, G.O., Converso, T.R., Politano, W.R., Ferraz, L.F.C., Ribeiro, M.L., Leite, L.C.C., and Darrieux, M. (2017). Role of Streptococcus pneumoniae proteins in evasion of complement-mediated immunity. Front. Microbiol., 8.","DOI":"10.3389\/fmicb.2017.00224"},{"key":"ref_386","doi-asserted-by":"crossref","unstructured":"Domenech, M., Sempere, J., de Miguel, S., and Yuste, J. (2018). Combination of antibodies and antibiotics as a promising strategy against multidrug-resistant pathogens of the respiratory tract. Front. Immunol., 9.","DOI":"10.3389\/fimmu.2018.02700"},{"key":"ref_387","doi-asserted-by":"crossref","unstructured":"Gil, E., Noursadeghi, M., and Brown, J.S. (2022). Streptococcus pneumoniae interactions with the complement system. Front. Cell. Infect. Microbiol., 12.","DOI":"10.3389\/fcimb.2022.929483"},{"key":"ref_388","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/S0092-8674(00)00138-0","article-title":"Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLeX and PSGL-1","volume":"103","author":"Somers","year":"2000","journal-title":"Cell"},{"key":"ref_389","doi-asserted-by":"crossref","unstructured":"Ramos-Sevillano, E., Urzainqui, A., de Andr\u00e9s, B., Gonz\u00e1lez-Tajuelo, R., Domenech, M., Gonz\u00e1lez-Camacho, F., S\u00e1nchez-Madrid, F., Brown, J.S., Garc\u00eda, E., and Yuste, J. (2016). PSGL-1 on leukocytes is a critical component of the host immune response against invasive pneumococcal disease. PLoS Pathog., 12.","DOI":"10.1371\/journal.ppat.1005500"},{"key":"ref_390","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1007\/978-94-017-8881-6_8","article-title":"The biology of pneumolysin","volume":"80","author":"Mitchell","year":"2014","journal-title":"Subcell. Biochem."},{"key":"ref_391","doi-asserted-by":"crossref","unstructured":"Cima Cabal, M.D., Molina, F., L\u00f3pez-S\u00e1nchez, J.I., P\u00e9rez-Sant\u00edn, E., and Garc\u00eda-Su\u00e1rez, M.d.M. (2023). Pneumolysin as a target for new therapies against pneumococcal infections: A systematic review. PLoS ONE, 18.","DOI":"10.1371\/journal.pone.0282970"},{"key":"ref_392","doi-asserted-by":"crossref","unstructured":"Anderson, R., and Feldman, C. (2023). The global burden of community-acquired pneumonia in adults, encompassing invasive pneumococcal disease and the prevalence of its associated cardiovascular events, with a focus on pneumolysin and macrolide antibiotics in pathogenesis and therapy. Int. J. Mol. Sci, 24.","DOI":"10.20944\/preprints202305.2086.v1"},{"key":"ref_393","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1097\/QCO.0000000000001010","article-title":"Bacterial cholesterol-dependent cytolysins and their interaction with the human immune response","volume":"37","author":"Sanford","year":"2024","journal-title":"Curr. Opin. Infect. Dis."},{"key":"ref_394","doi-asserted-by":"crossref","first-page":"4079","DOI":"10.1128\/IAI.01747-07","article-title":"Pneumolysin released during Streptococcus pneumoniae autolysis is a potent activator of intracellular oxygen radical production in neutrophils","volume":"76","author":"Martner","year":"2008","journal-title":"Infect. Immun."},{"key":"ref_395","doi-asserted-by":"crossref","first-page":"1892","DOI":"10.1038\/s41467-020-15751-6","article-title":"Increased pathogenicity of pneumococcal serotype 1 is driven by rapid autolysis and release of pneumolysin","volume":"11","author":"Jacques","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_396","doi-asserted-by":"crossref","first-page":"3651","DOI":"10.1128\/JB.00114-12","article-title":"Export requirements of pneumolysin in Streptococcus pneumoniae","volume":"194","author":"Price","year":"2012","journal-title":"J. Bacteriol."},{"key":"ref_397","doi-asserted-by":"crossref","unstructured":"Bryant, J.C., Dabbs, R.C., Oswalt, K.L., Brown, L.R., Rosch, J.W., Seo, K.S., Donaldson, J.R., McDaniel, L.S., and Thornton, J.A. (2016). Pyruvate oxidase of Streptococcus pneumoniae contributes to pneumolysin release. BMC Microbiol., 16.","DOI":"10.1186\/s12866-016-0881-6"},{"key":"ref_398","doi-asserted-by":"crossref","unstructured":"Bazant, J., Ott, B., Hudel, M., Hain, T., Lucas, R., and Mraheil, M.A. (2023). Impact of endogenous pneumococcal hydrogen peroxide on the activity and release of pneumolysin. Toxins, 15.","DOI":"10.3389\/fimmu.2024.1414195"},{"key":"ref_399","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1111\/j.1365-2958.2008.06294.x","article-title":"A new twist on an old pathway-accessory Sec systems","volume":"69","author":"Rigel","year":"2008","journal-title":"Mol. Microbiol."},{"key":"ref_400","doi-asserted-by":"crossref","unstructured":"Braunstein, M., Bensing, B., and Sullam, P.M. (2019). The two distinct types of SecA2-dependent export systems. Microbiol. Spectr., 7.","DOI":"10.1128\/microbiolspec.PSIB-0025-2018"},{"key":"ref_401","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1016\/j.micinf.2017.04.003","article-title":"The accessory Sec system (SecY2A2) in Streptococcus pneumoniae is involved in export of pneumolysin toxin, adhesion and biofilm formation","volume":"19","author":"Bandara","year":"2017","journal-title":"Microbes Infect."},{"key":"ref_402","doi-asserted-by":"crossref","first-page":"e0005622","DOI":"10.1128\/iai.00056-22","article-title":"The major autolysin Atl regulates the virulence of Staphylococcus aureus by controlling the sorting of LukAB","volume":"90","author":"Zheng","year":"2022","journal-title":"Infect. Immun."},{"key":"ref_403","doi-asserted-by":"crossref","first-page":"e01309-21","DOI":"10.1128\/mBio.01309-21","article-title":"A novel aquaporin subfamily imports oxygen and contributes to pneumococcal virulence by controlling the production and release of virulence factors","volume":"12","author":"Hu","year":"2021","journal-title":"mBio"},{"key":"ref_404","doi-asserted-by":"crossref","unstructured":"Satala, D., Bednarek, A., Kozik, A., Rapala-Kozik, M., and Karkowska-Kuleta, J. (2023). The recruitment and activation of plasminogen by bacteria\u2013The involvement in chronic infection development. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241310436"},{"key":"ref_405","doi-asserted-by":"crossref","unstructured":"Jeffery, C.J. (2018). Protein moonlighting: What is it, and why is it important?. Philos. Trans. R. Soc. Lond. B Biol. Sci., 373.","DOI":"10.1098\/rstb.2016.0523"},{"key":"ref_406","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1007\/s00018-023-04781-0","article-title":"Moonlighting enzymes: When cellular context defines specificity","volume":"80","author":"Gupta","year":"2023","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_407","doi-asserted-by":"crossref","first-page":"2551","DOI":"10.1021\/acsinfecdis.4c00323","article-title":"Anchorless bacterial moonlighting metabolic enzymes modulate the immune system and contribute to pathogenesis","volume":"10","author":"Liu","year":"2024","journal-title":"ACS Infect. Dis."},{"key":"ref_408","doi-asserted-by":"crossref","first-page":"304","DOI":"10.2174\/1389203719666181026170751","article-title":"Medical and veterinary importance of the moonlighting functions of triosephosphate isomerase","volume":"20","year":"2019","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_409","doi-asserted-by":"crossref","first-page":"1206","DOI":"10.1002\/2211-5463.13396","article-title":"Triosephosphate isomerase of Streptococcus pneumoniae is released extracellularly by autolysis and binds to host plasminogen to promote its activation","volume":"12","author":"Hirayama","year":"2022","journal-title":"FEBS Open Bio."},{"key":"ref_410","doi-asserted-by":"crossref","unstructured":"Hirayama, S., Hiyoshi, T., Yasui, Y., Domon, H., and Terao, Y. (2023). C-terminal lysine residue of pneumococcal triosephosphate isomerase contributes to its binding to host plasminogen. Microorganisms, 11.","DOI":"10.3390\/microorganisms11051198"},{"key":"ref_411","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1128\/IAI.72.4.2416-2419.2004","article-title":"Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein","volume":"72","author":"Bergmann","year":"2004","journal-title":"Infect. Immun."},{"key":"ref_412","doi-asserted-by":"crossref","first-page":"5350","DOI":"10.1128\/IAI.00184-08","article-title":"The interaction of Streptococcus pneumoniae with plasmin mediates transmigration across endothelial and epithelial monolayers by intercellular junction cleavage","volume":"76","author":"Attali","year":"2008","journal-title":"Infect. Immun."},{"key":"ref_413","doi-asserted-by":"crossref","unstructured":"Terrasse, R., Amoroso, A., Vernet, T., and Di Guilmi, A.M. (2015). Streptococcus pneumoniae GAPDH is released by cell lysis and interacts with peptidoglycan. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0125377"},{"key":"ref_414","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1080\/21505594.2021.1889812","article-title":"Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases","volume":"12","author":"Marquart","year":"2021","journal-title":"Virulence"},{"key":"ref_415","doi-asserted-by":"crossref","first-page":"15833","DOI":"10.1074\/jbc.M113.530212","article-title":"Binding of Streptococcus pneumoniae endopeptidase O (PepO) to complement component C1q modulates the complement attack and promotes host cell adherence","volume":"289","author":"Agarwal","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_416","doi-asserted-by":"crossref","unstructured":"Harvey, K.L., Jarocki, V.M., Charles, I.G., and Djordjevic, S.P. (2019). The diverse functional roles of elongation factor Tu (EF-Tu) in microbial pathogenesis. Front. Microbiol., 10.","DOI":"10.3389\/fmicb.2019.02351"},{"key":"ref_417","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1007\/s00284-013-0422-6","article-title":"How are the non-classically secreted bacterial proteins released into the extracellular milieu?","volume":"67","author":"Wang","year":"2013","journal-title":"Curr. Microbiol."},{"key":"ref_418","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/j.molimm.2014.06.029","article-title":"Tuf of Streptococcus pneumoniae is a surface displayed human complement regulator binding protein","volume":"62","author":"Mohan","year":"2014","journal-title":"Mol. Immunol."},{"key":"ref_419","doi-asserted-by":"crossref","first-page":"10859","DOI":"10.1038\/ncomms10859","article-title":"Dynamic capsule restructuring by the main pneumococcal autolysin LytA in response to the epithelium","volume":"7","author":"Kietzman","year":"2016","journal-title":"Nat. Commun."},{"key":"ref_420","doi-asserted-by":"crossref","unstructured":"Ridyard, K.E., and Overhage, J. (2021). The potential of human peptide LL-37 as an antimicrobial and anti-biofilm agent. Antibiotics, 10.","DOI":"10.3390\/antibiotics10060650"},{"key":"ref_421","doi-asserted-by":"crossref","unstructured":"Souza Guerra, M.E., Vieira, B., Carvalho Thiers Calazans, A.P., Destro, G.V., Melo, K., Rodrigues, E., Waz, N.T., Girardello, R., Darrieux, M., and Converso, T.R. (2024). Recent advances in the therapeutic potential of cathelicidins. Front. Microbiol., 15.","DOI":"10.3389\/fmicb.2024.1405760"},{"key":"ref_422","doi-asserted-by":"crossref","first-page":"4653","DOI":"10.1128\/IAI.73.8.4653-4667.2005","article-title":"Illustration of pneumococcal polysaccharide capsule during adherence and invasion of epithelial cells","volume":"73","author":"Hammerschmidt","year":"2005","journal-title":"Infect. Immun."},{"key":"ref_423","doi-asserted-by":"crossref","first-page":"3877","DOI":"10.1099\/mic.0.2008\/022301-0","article-title":"Capsule polysaccharide is a bacterial decoy for antimicrobial peptides","volume":"154","author":"Llobet","year":"2008","journal-title":"Microbiology"},{"key":"ref_424","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1111\/j.1600-065X.2011.01082.x","article-title":"\u03b2-Defensins in human innate immunity","volume":"245","author":"Lehrer","year":"2012","journal-title":"Immunol. Rev."},{"key":"ref_425","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1038\/s41392-023-01553-x","article-title":"Mechanisms and regulation of defensins in host defense","volume":"8","author":"Fu","year":"2023","journal-title":"Signal Transduct. Target Ther."},{"key":"ref_426","doi-asserted-by":"crossref","first-page":"3710","DOI":"10.1128\/IAI.01748-07","article-title":"The capsule sensitizes Streptococcus pneumoniae to \u03b1-defensins human neutrophil proteins 1 to 3","volume":"76","author":"Beiter","year":"2008","journal-title":"Infect. Immun."},{"key":"ref_427","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1165\/rcmb.2014-0024OC","article-title":"Role of pneumococcal autolysin for KLF4 expression and chemokine secretion in lung epithelium","volume":"53","author":"Zahlten","year":"2015","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"ref_428","doi-asserted-by":"crossref","first-page":"1822","DOI":"10.1093\/infdis\/jiu806","article-title":"Streptococcus pneumoniae-induced oxidative stress in lung epithelial cells depends on pneumococcal autolysis and is reversible by resveratrol","volume":"211","author":"Zahlten","year":"2015","journal-title":"J. Infect. Dis."},{"key":"ref_429","doi-asserted-by":"crossref","first-page":"107345","DOI":"10.1016\/j.phrs.2024.107345","article-title":"A review of KLF4 and inflammatory disease: Current status and future perspective","volume":"207","author":"Liang","year":"2024","journal-title":"Pharmacol. Res."},{"key":"ref_430","doi-asserted-by":"crossref","first-page":"148027","DOI":"10.1016\/j.gene.2023.148027","article-title":"The kruppel-like factor (KLF) family, diseases, and physiological events","volume":"895","author":"Yuce","year":"2024","journal-title":"Gene"},{"key":"ref_431","doi-asserted-by":"crossref","unstructured":"Herta, T., Bhattacharyya, A., Bollensdorf, C., Kabus, C., Garc\u00eda, P., Suttorp, N., Hippenstiel, S., and Zahlten, J. (2018). DNA-release by Streptococcus pneumoniae autolysin LytA induced Krueppel-like factor 4 expression in macrophages. Sci. Rep., 8.","DOI":"10.1038\/s41598-018-24152-1"},{"key":"ref_432","doi-asserted-by":"crossref","unstructured":"Herta, T., Bhattacharyya, A., Rosolowski, M., Conrad, C., Gurtner, C., Gruber, A.D., Ahnert, P., Gutbier, B., Frey, D., and Suttorp, N. (2021). Krueppel-like factor 4 expression in phagocytes regulates early inflammatory response and disease severity in pneumococcal pneumonia. Front. Immunol., 12.","DOI":"10.3389\/fimmu.2021.726135"},{"key":"ref_433","doi-asserted-by":"crossref","unstructured":"Bhattacharyya, A., Herta, T., Conrad, C., Frey, D., Garc\u00eda, P., Suttorp, N., Hippenstiel, S., and Zahlten, J. (2021). Induction of Kr\u00fcppel-like factor 4 mediates polymorphonuclear neutrophil activation in Streptococcus pneumoniae infection. Front. Microbiol., 11.","DOI":"10.3389\/fmicb.2020.582070"},{"key":"ref_434","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1093\/jleuko\/qiad070","article-title":"Neutrophil responsiveness to IL-10 impairs clearance of Streptococcus pneumoniae from the lungs","volume":"115","author":"Horn","year":"2024","journal-title":"J. Leukoc. Biol."},{"key":"ref_435","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1093\/jleuko\/qiad134","article-title":"Neutrophils sing \u201cIL[-10] be seeing you\u201d in the lungs during pneumonia","volume":"115","author":"McPeek","year":"2024","journal-title":"J. Leukoc. Biol."},{"key":"ref_436","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.ijmm.2014.12.002","article-title":"Stress-triggered signaling affecting survival or suicide of Streptococcus pneumoniae","volume":"305","author":"Cortes","year":"2015","journal-title":"Int. J. Med. Microbiol."},{"key":"ref_437","doi-asserted-by":"crossref","first-page":"3935","DOI":"10.1099\/mic.0.28238-0","article-title":"Transcriptional analysis of the acid tolerance response in Streptococcus pneumoniae","volume":"151","author":"Overweg","year":"2005","journal-title":"Microbiology"},{"key":"ref_438","doi-asserted-by":"crossref","first-page":"1300","DOI":"10.1099\/mic.0.2007\/015925-0","article-title":"Acidic stress induces autolysis by a CSP-independent ComE pathway in Streptococcus pneumoniae","volume":"154","author":"Cortes","year":"2008","journal-title":"Microbiology"},{"key":"ref_439","doi-asserted-by":"crossref","unstructured":"Pi\u00f1as, G.E., Reinoso-Vizcaino, N.M., Yandar Barahona, N.Y., Cortes, P.R., Duran, R., Badapanda, C., Rathore, A., Bichara, D.R., Cian, M.B., and Olivero, N.B. (2018). Crosstalk between the serine\/threonine kinase StkP and the response regulator ComE controls the stress response and intracellular survival of Streptococcus pneumoniae. PLoS Pathog., 14.","DOI":"10.1371\/journal.ppat.1007118"},{"key":"ref_440","doi-asserted-by":"crossref","unstructured":"Reinoso-Vizca\u00edno, N.M., Cian, M.B., Cortes, P.R., Olivero, N.B., Hernandez-Morfa, M., Pi\u00f1as, G.E., Badapanda, C., Rathore, A., Perez, D.R., and Echenique, J. (2020). The pneumococcal two-component system SirRH is linked to enhanced intracellular survival of Streptococcus pneumoniae in influenza-infected pulmonary cells. PLoS Pathog., 16.","DOI":"10.1371\/journal.ppat.1008761"},{"key":"ref_441","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1042\/EBC20240019","article-title":"A comparative guide to expression systems for phage lysin production","volume":"68","author":"Cremelie","year":"2024","journal-title":"Essays Biochem."},{"key":"ref_442","doi-asserted-by":"crossref","unstructured":"Mart\u00edn-Galiano, A.J., and Garc\u00eda, E. (2021). Streptococcus pneumoniae: A plethora of temperate bacteriophages with a role in host genome rearrangement. Front. Cell. Infect. Microbiol., 11.","DOI":"10.3389\/fcimb.2021.775402"},{"key":"ref_443","doi-asserted-by":"crossref","unstructured":"V\u00e1zquez, R., Garc\u00eda, E., and Garc\u00eda, P. (2018). Phage lysins for fighting bacterial respiratory infections: A new generation of antimicrobials. Front. Immunol., 9.","DOI":"10.3389\/fimmu.2018.02252"},{"key":"ref_444","doi-asserted-by":"crossref","unstructured":"Liu, H., Hu, Z., Li, M., Yang, Y., Lu, S., and Rao, X. (2023). Therapeutic potential of bacteriophage endolysins for infections caused by Gram-positive bacteria. J. Biomed. Sci., 30.","DOI":"10.1186\/s12929-023-00919-1"},{"key":"ref_445","doi-asserted-by":"crossref","first-page":"4162","DOI":"10.1073\/pnas.72.10.4162","article-title":"Mechanism of action of penicillin: Triggering of the pneumococcal autolytic enzyme by inhibitors of cell wall synthesis","volume":"72","author":"Tomasz","year":"1975","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"ref_446","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1093\/jac\/dkm342","article-title":"In vitro interactions of LytA, the major pneumococcal autolysin, with two bacteriophage lytic enzymes (Cpl-1 and Pal), cefotaxime and moxifloxacin against antibiotic-susceptible and -resistant Streptococcus pneumoniae strains","volume":"60","author":"Gracia","year":"2007","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_447","doi-asserted-by":"crossref","first-page":"3371","DOI":"10.1128\/AAC.00137-07","article-title":"Pneumococcal LytA autolysin, a potent therapeutic agent in experimental peritonitis-sepsis caused by highly \u03b2-lactam-resistant Streptococcus pneumoniae","volume":"51","author":"Huelves","year":"2007","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_448","doi-asserted-by":"crossref","first-page":"4144","DOI":"10.1128\/AAC.00492-11","article-title":"In vitro destruction of Streptococcus pneumoniae biofilms with bacterial and phage peptidoglycan hydrolases","volume":"55","author":"Domenech","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_449","doi-asserted-by":"crossref","first-page":"5516","DOI":"10.1128\/jb.174.17.5516-5525.1992","article-title":"EJ-1, a temperate bacteriophage of Streptococcus pneumoniae with a Myoviridae morphotype","volume":"174","year":"1992","journal-title":"J. Bacteriol."},{"key":"ref_450","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/j.virol.2004.01.029","article-title":"Genomic organization and molecular analysis of the inducible prophage EJ-1, a mosaic myovirus from an atypical pneumococcus","volume":"322","author":"Romero","year":"2004","journal-title":"Virology"},{"key":"ref_451","doi-asserted-by":"crossref","unstructured":"Le, C.-F., Yusof, M.Y.M., Hassan, M.A.A., Lee, V.S., Isa, D.M., and Sekaran, S.D. (2015). In vivo efficacy and molecular docking of designed peptide that exhibits potent antipneumococcal activity and synergises in combination with penicillin. Sci. Rep., 5.","DOI":"10.1038\/srep11886"},{"key":"ref_452","doi-asserted-by":"crossref","unstructured":"Hern\u00e1ndez-Ortiz, N., S\u00e1nchez-Murcia, P.A., Gil-Campillo, C., Domenech, M., Lucena-Agell, D., Hortig\u00fcela, R., Vel\u00e1zquez, S., Camarasa, M.J., Bustamante, N., and de Castro, S. (2024). Design, synthesis and structure-activity relationship (SAR) studies of an unusual class of non-cationic fatty amine-tripeptide conjugates as novel synthetic antimicrobial agents. Front. Pharmacol., 15.","DOI":"10.3389\/fphar.2024.1428409"},{"key":"ref_453","doi-asserted-by":"crossref","unstructured":"Tafroji, W., Margyaningsih, N.I., Khoeri, M.M., Paramaiswari, W.T., Winarti, Y., Salsabila, K., Putri, H.F.M., Siregar, N.C., Soebandrio, A., and Safari, D. (2022). Antibacterial activity of medicinal plants in Indonesia on Streptococcus pneumoniae. PLoS ONE, 17.","DOI":"10.1371\/journal.pone.0274174"},{"key":"ref_454","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1186\/s13568-024-01736-x","article-title":"Coptis rhizome extract influence on Streptococcus pneumoniae through autolysin activation","volume":"14","author":"Lee","year":"2024","journal-title":"AMB Express"},{"key":"ref_455","doi-asserted-by":"crossref","first-page":"e03027-20","DOI":"10.1128\/mBio.03027-20","article-title":"The bactericidal fatty acid mimetic 2CCA-1 selectively targets pneumococcal extracellular polyunsaturated fatty acid metabolism","volume":"11","author":"Reithuber","year":"2020","journal-title":"mBio"},{"key":"ref_456","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1084\/jem.13.1.1","article-title":"Chemo-immunological studies on localized infections. Fist paper: Action on the pneumococcus and its experimental infections of combined sodium oleate and antipneumococcal serum","volume":"13","author":"Lamar","year":"1911","journal-title":"J. Exp. Med."},{"key":"ref_457","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1128\/AAC.2.1.23","article-title":"Fatty acids and derivatives as antimicrobial agents","volume":"2","author":"Kabara","year":"1972","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_458","doi-asserted-by":"crossref","first-page":"1844","DOI":"10.1128\/AAC.01428-06","article-title":"In vitro bactericidal activity of the antiprotozoal drug miltefosine against Streptococcus pneumoniae and other pathogenic streptococci","volume":"51","author":"Llull","year":"2007","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_459","doi-asserted-by":"crossref","first-page":"3723","DOI":"10.1128\/AAC.01597-09","article-title":"Screen for inducers of autolysis in Bacillus subtilis","volume":"54","author":"Falk","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_460","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1039\/D4CB00106K","article-title":"Miltefosine impacts small molecule transport in Gram-positive bacteria","volume":"5","author":"Blake","year":"2024","journal-title":"RSC Chem. Biol."},{"key":"ref_461","doi-asserted-by":"crossref","first-page":"6274","DOI":"10.1128\/AAC.00653-15","article-title":"Bactericidal activity of ceragenin CSA-13 in cell culture and in an animal model of peritoneal infection","volume":"59","author":"Bucki","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_462","doi-asserted-by":"crossref","unstructured":"Moscoso, M., Esteban-Torres, M., Men\u00e9ndez, M., and Garc\u00eda, E. (2014). In vitro bactericidal and bacteriolytic activity of ceragenin CSA-13 against planktonic cultures and biofilms of Streptococcus pneumoniae and other pathogenic streptococci. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0101037"},{"key":"ref_463","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1093\/jac\/dks434","article-title":"Antibacterial activity of the human host defence peptide LL-37 and selected synthetic cationic lipids against bacteria associated with oral and upper respiratory tract infections","volume":"68","author":"Namiot","year":"2013","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_464","doi-asserted-by":"crossref","unstructured":"Oyardi, O., Savage, P.B., and Guzel, C.B. (2022). Effects of ceragenins and antimicrobial peptides on the A549 cell line and an in vitro co-culture model of A549 cells and Pseudomonas aeruginosa. Pathogens, 11.","DOI":"10.3390\/pathogens11091044"},{"key":"ref_465","doi-asserted-by":"crossref","unstructured":"Karasi\u0144ski, M., Wnorowska, U., Durna\u015b, B., Kr\u00f3l, G., Daniluk, T., Sk\u0142odowski, K., G\u0142uszek, K., Piktel, E., Ok\u0142a, S., and Bucki, R. (2023). Ceragenins and ceragenin-based core-shell nanosystems as new antibacterial agents against Gram-negative rods causing nosocomial infections. Pathogens, 12.","DOI":"10.3390\/pathogens12111346"},{"key":"ref_466","doi-asserted-by":"crossref","first-page":"2624","DOI":"10.1128\/JB.01501-09","article-title":"Evidence of localized prophage-host recombination in the lytA gene encoding the major pneumococcal autolysin","volume":"192","author":"Morales","year":"2010","journal-title":"J. Bacteriol."},{"key":"ref_467","doi-asserted-by":"crossref","first-page":"4551","DOI":"10.1128\/IAI.67.9.4551-4556.1999","article-title":"The autolysin-encoding gene (lytA) of Streptococcus pneumoniae displays restricted allelic variation despite localized recombination events with genes of pneumococcal bacteriophage encoding cell wall lytic enzymes","volume":"67","author":"Whatmore","year":"1999","journal-title":"Infect. Immun."},{"key":"ref_468","doi-asserted-by":"crossref","first-page":"5064","DOI":"10.1128\/jb.172.9.5064-5070.1990","article-title":"Sequence of the Streptococcus pneumoniae bacteriophage HB-3 amidase reveals high homology with the major host autolysin","volume":"172","author":"Romero","year":"1990","journal-title":"J. Bacteriol."},{"key":"ref_469","doi-asserted-by":"crossref","unstructured":"Didelot, X., Davison, C., Tallman, S., de Ste-Croix, M., Antonio, M., Oggioni, M.R., Kwambana-Adams, B., Freund, F., and Beleza, S. (2024). Long-term evolution of Streptococcus mitis and Streptococcus pneumoniae leads to higher genetic diversity within rather than between human populations. PLoS Genet., 20.","DOI":"10.1371\/journal.pgen.1011317"},{"key":"ref_470","doi-asserted-by":"crossref","first-page":"126656","DOI":"10.1016\/j.vaccine.2024.126656","article-title":"Systematic literature review of cost-effectiveness analyses of adult 15- and 20-valent pneumococcal vaccines","volume":"46","author":"Cho","year":"2025","journal-title":"Vaccine"},{"key":"ref_471","doi-asserted-by":"crossref","unstructured":"Sempere, J., Llamos\u00ed, M., del R\u00edo Men\u00e9ndez, I., L\u00f3pez Ruiz, B., Domenech, M., and Gonz\u00e1lez-Camacho, F. (2021). Pneumococcal choline-binding proteins involved in virulence as vaccine candidates. Vaccines, 9.","DOI":"10.3390\/vaccines9020181"},{"key":"ref_472","doi-asserted-by":"crossref","unstructured":"Silva, P.H., V\u00e1zquez, Y., Campusano, C., Retamal-D\u00edaz, A., Lay, M.K., Mu\u00f1oz, C.A., Gonz\u00e1lez, P.A., Kalergis, A.M., and Bueno, S.M. (2022). Non-capsular based immunization approaches to prevent Streptococcus pneumoniae infection. Front. Cell. Infect. Microbiol., 12.","DOI":"10.3389\/fcimb.2022.949469"},{"key":"ref_473","doi-asserted-by":"crossref","unstructured":"Li, S., Liang, H., Zhao, S.H., Yang, X.Y., and Guo, Z. (2023). Recent progress in pneumococcal protein vaccines. Front. Immunol., 14.","DOI":"10.3389\/fimmu.2023.1278346"},{"key":"ref_474","doi-asserted-by":"crossref","unstructured":"Wang, Y., Shi, G., Wang, X., Xie, Z., Gou, J., Huang, L., Huang, H., You, W., Wang, R., and Yang, Y. (2024). Preliminary evaluation of the safety and immunogenicity of a novel protein-based pneumococcal vaccine in healthy adults aged 18\u201349: A phase Ia randomized, double blind, placebo-controlled clinical study. Vaccines, 12.","DOI":"10.3390\/vaccines12080827"},{"key":"ref_475","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/0882-4010(92)90116-6","article-title":"Comparative efficacy of autolysin and pneumolysin as immunogens protecting mice against infection by Streptococcus pneumoniae","volume":"12","author":"Lock","year":"1992","journal-title":"Microb. Pathog."},{"key":"ref_476","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1007\/s12026-011-8234-x","article-title":"Intranasal immunization with autolysin (LytA) in mice model induced protection against five prevalent Streptococcus pneumoniae serotypes in China","volume":"51","author":"Yuan","year":"2011","journal-title":"Immunol. Res."},{"key":"ref_477","doi-asserted-by":"crossref","unstructured":"Corsini, B., Aguinagalde, L., Ruiz, S., Domenech, M., and Yuste, J. (2021). Vaccination with LytA, LytC, or Pce of Streptococcus pneumoniae protects against sepsis by inducing IgGs that activate the complement system. Vaccines, 9.","DOI":"10.3390\/vaccines9020186"},{"key":"ref_478","doi-asserted-by":"crossref","first-page":"76","DOI":"10.7774\/cevr.2020.9.2.76","article-title":"Autolysin (lytA) recombinant protein: A potential target for developing vaccines against pneumococcal infections","volume":"9","author":"Afshar","year":"2020","journal-title":"Clin. Exp. Vaccine Res."},{"key":"ref_479","doi-asserted-by":"crossref","unstructured":"van Dalen, R., Elsherbini, A.M.A., Harms, M., Alber, S., Stemmler, R., and Peschel, A. (2023). Secretory IgA impacts the microbiota density in the human nose. Microbiome, 11.","DOI":"10.1186\/s40168-023-01675-y"},{"key":"ref_480","doi-asserted-by":"crossref","first-page":"1901539","DOI":"10.1183\/13993003.01539-2019","article-title":"Can animal models really teach us anything about pneumonia? Pro","volume":"55","author":"Orihuela","year":"2020","journal-title":"Eur. Respir. J."},{"key":"ref_481","doi-asserted-by":"crossref","first-page":"1901525","DOI":"10.1183\/13993003.01525-2019","article-title":"Can animal models really teach us anything about pneumonia? Con","volume":"55","author":"Metersky","year":"2020","journal-title":"Eur. Respir. J."},{"key":"ref_482","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1084\/jem.20011576","article-title":"The immune response to pneumococcal proteins during experimental human carriage","volume":"195","author":"McCool","year":"2002","journal-title":"J. Exp. Med."},{"key":"ref_483","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1016\/j.tim.2011.06.003","article-title":"Experimental human pneumococcal carriage models for vaccine research","volume":"19","author":"Ferreira","year":"2011","journal-title":"Trends Microbiol."},{"key":"ref_484","doi-asserted-by":"crossref","first-page":"2","DOI":"10.12688\/wellcomeopenres.19949.1","article-title":"Experimental pneumococcal carriage in people living with HIV in Malawi: The first controlled human infection model in a key at-risk population","volume":"9","author":"Doherty","year":"2024","journal-title":"Wellcome Open Res."},{"key":"ref_485","doi-asserted-by":"crossref","first-page":"e075948","DOI":"10.1136\/bmjopen-2023-075948","article-title":"Serotype 3 Experimental Human Pneumococcal Challenge (EHPC) study protocol: Dose ranging and reproducibility in a healthy volunteer population (challenge 3)","volume":"14","author":"Hazenberg","year":"2024","journal-title":"BMJ Open"},{"key":"ref_486","doi-asserted-by":"crossref","unstructured":"Masomian, M., Ahmad, Z., Gew, L.T., and Poh, C.L. (2020). Development of next generation Streptococcus pneumoniae vaccines conferring broad protection. Vaccines, 8.","DOI":"10.3390\/vaccines8010132"}],"container-title":["Microorganisms"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-2607\/13\/4\/827\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T17:10:56Z","timestamp":1760029856000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-2607\/13\/4\/827"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,4,5]]},"references-count":486,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2025,4]]}},"alternative-id":["microorganisms13040827"],"URL":"https:\/\/doi.org\/10.3390\/microorganisms13040827","relation":{},"ISSN":["2076-2607"],"issn-type":[{"value":"2076-2607","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,4,5]]}}}