{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T14:54:57Z","timestamp":1790434497142,"version":"4.1.0"},"reference-count":146,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2020,7,27]],"date-time":"2020-07-27T00:00:00Z","timestamp":1595808000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Virginia Commonwealth University Clinical &amp; Translational Science Award","award":["UL1TR002649"],"award-info":[{"award-number":["UL1TR002649"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antibodies"],"abstract":"<jats:p>Pathogenic bacteria are a global health threat, with over 2 million infections caused by Gram-negative bacteria every year in the United States. This problem is exacerbated by the increase in resistance to common antibiotics that are routinely used to treat these infections, creating an urgent need for innovative ways to treat and prevent virulence caused by these pathogens. Many Gram-negative pathogenic bacteria use a type III secretion system (T3SS) to inject toxins and other effector proteins directly into host cells. The T3SS has become a popular anti-virulence target because it is required for pathogenesis and knockouts have attenuated virulence. It is also not required for survival, which should result in less selective pressure for resistance formation against T3SS inhibitors. In this review, we will highlight selected examples of direct antibody immunizations and the use of antibodies in immunotherapy treatments that target the bacterial T3SS. These examples include antibodies targeting the T3SS of Pseudomonas aeruginosa, Yersinia pestis, Escherichia coli, Salmonella enterica, Shigella spp., and Chlamydia trachomatis.<\/jats:p>","DOI":"10.3390\/antib9030035","type":"journal-article","created":{"date-parts":[[2020,7,27]],"date-time":"2020-07-27T04:39:50Z","timestamp":1595824790000},"page":"35","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":35,"title":["Antibodies Inhibiting the Type III Secretion System of Gram-Negative Pathogenic Bacteria"],"prefix":"10.3390","volume":"9","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2427-5482","authenticated-orcid":false,"given":"Julia A.","family":"Hotinger","sequence":"first","affiliation":[{"name":"Department of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, Richmond, VA 23219, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aaron E.","family":"May","sequence":"additional","affiliation":[{"name":"Department of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, Richmond, VA 23219, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,7,27]]},"reference":[{"key":"ref_1","first-page":"245","article-title":"The injectisome, a complex nanomachine for protein injection into mammalian cells","volume":"8","year":"2019","journal-title":"EcoSal Plus"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"3879","DOI":"10.1111\/1462-2920.13755","article-title":"A global survey of bacterial type III secretion systems and their effectors","volume":"19","author":"Hu","year":"2017","journal-title":"Environ. Microbiol."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Pendergrass, H.A., and May, A.E. (2019). Natural product type III secretion system inhibitors. Antibiotics, 8.","DOI":"10.3390\/antibiotics8040162"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1146\/annurev.micro.54.1.735","article-title":"Assembly and function of type III secretory systems","volume":"54","author":"Cornelis","year":"2000","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1111\/mmi.12843","article-title":"Three-dimensional electron microscopy reconstruction and cysteine-mediated crosslinking provide a model of the type III secretion system needle tip complex","volume":"95","author":"Cheung","year":"2015","journal-title":"Mol. Microbiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"348","DOI":"10.3389\/fcimb.2017.00348","article-title":"Swiss army pathogen: The Salmonella entry toolkit","volume":"7","author":"Hume","year":"2017","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"64","DOI":"10.3389\/fcimb.2017.00064","article-title":"How do the virulence factors of Shigella work together to cause disease?","volume":"7","author":"Mattock","year":"2017","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"5","DOI":"10.5604\/17331331.1197324","article-title":"The functions of effector proteins in Yersinia virulence","volume":"65","author":"Zhang","year":"2016","journal-title":"Pol. J. Microbiol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"L337","DOI":"10.1152\/ajplung.00103.2015","article-title":"Pseudomonas aeruginosa exoenzymes U and Y induce a transmissible endothelial proteinopathy","volume":"310","author":"Morrow","year":"2016","journal-title":"Am. J. Physiol. Lung Cell Mol. Physiol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1517\/14728222.2014.855199","article-title":"Targeting the type III secretion system to treat bacterial infections","volume":"18","author":"Marshall","year":"2014","journal-title":"Expert Opin. Ther. Targets"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1038\/s41564-019-0368-y","article-title":"Export of a Vibrio parahaemolyticus toxin by the Sec and type III secretion machineries in tandem","volume":"4","author":"Matsuda","year":"2019","journal-title":"Nat. Microbiol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"21","DOI":"10.3389\/fmicb.2011.00021","article-title":"Chlamydia pneumoniae CdsL regulates CdsN ATPase activity, and disruption with a peptide mimetic prevents bacterial invasion","volume":"2","author":"Stone","year":"2011","journal-title":"Front. Microbiol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"e00093","DOI":"10.1128\/mSphere.00093-19","article-title":"Horiguchi YBspR\/BtrA, an anti-\u03c3, factor. Regulates the ability of Bordetella bronchiseptica to cause cough in rats","volume":"4","author":"Nakamura","year":"2019","journal-title":"Msphere"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"e01202","DOI":"10.1128\/AAC.01202-17","article-title":"Impact of type III secretion effectors and of phenoxyacetamide inhibitors of type III Secretion on abscess formation in a mouse model of Pseudomonas aeruginosa infection","volume":"61","author":"Berube","year":"2017","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"5433","DOI":"10.1128\/AAC.00975-12","article-title":"Chemical inhibitors of the type three secretion system: Disarming bacterial pathogens","volume":"56","author":"Duncan","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/S0924-8579(01)00317-X","article-title":"Antibiotic selective pressure and development of bacterial resistance","volume":"17","year":"2001","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1038\/ja.2010.155","article-title":"A small-molecule inhibitor of the bacterial type III secretion system protects against in vivo infection with Citrobacter rodentium","volume":"64","author":"Kimura","year":"2011","journal-title":"J. Antibiot."},{"key":"ref_18","first-page":"166","article-title":"Human colostrum contains IgA antibodies reactive to enteropathogenic Escherichia coli virulence-associated proteins: Intimin, BfpA, EspA, and EspB","volume":"27","author":"Loureiro","year":"1998","journal-title":"J. Pediatr. Gastroenterol. Nutr."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"e00412","DOI":"10.1128\/CVI.00412-16","article-title":"Functional and antigen-specific serum antibody levels as correlates of protection against shigellosis in a controlled human challenge study","volume":"24","author":"Shimanovich","year":"2017","journal-title":"Clin. Vaccine Immunol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.micpath.2013.09.001","article-title":"Identification of secretory immunoglobulin A antibody targets from human milk in cultured cells infected with enteropathogenic Escherichia coli (EPEC)","volume":"64","year":"2013","journal-title":"Microb. Pathog."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"5090","DOI":"10.1128\/IAI.68.9.5090-5095.2000","article-title":"Human response to Escherichia coli O157:H7 infection: Antibodies to secreted virulence factors","volume":"68","author":"Li","year":"2000","journal-title":"Infect. Immun."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1122","DOI":"10.1097\/INF.0b013e318293306c","article-title":"Detection of secretory immunoglobulin a in human colostrum as mucosal immune response against proteins of the type III secretion system of Salmonella, Shigella and enteropathogenic Escherichia coli","volume":"32","author":"Durand","year":"2013","journal-title":"Pediatr. Infect. Dis. J."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"3318","DOI":"10.3168\/jds.2011-5093","article-title":"Vaccination of pregnant cows with EspA, EspB, \u03b3-intimin, and Shiga toxin 2 proteins from Escherichia coli O157:H7 induces high levels of specific colostral antibodies that are transferred to newborn calves","volume":"95","author":"Rabinovitz","year":"2012","journal-title":"J. Dairy Sci."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"3823","DOI":"10.1016\/j.vaccine.2014.04.073","article-title":"Physiopathological effects of Escherichia coli O157: H7 inoculation in weaned calves fed with colostrum containing antibodies to EspB and Intimin","volume":"32","author":"Rabinovitz","year":"2014","journal-title":"Vaccine"},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Mendelow, B., Ramsay, M.N., and Chetty, W.S. (2009). Immunology. Molecular Medicine for Clinicians, Wits University Press.","DOI":"10.18772\/22008014655"},{"key":"ref_26","unstructured":"Morrow, W.J.W., Sheikh, N.A., Schmidt, C.S., and Davies, H.D. (2012). Antigen Discovery for Vaccines Using High-throughput Proteomic Screening Techniques. Vaccinology: Principles and Practice, Blackwell Publishing Ltd."},{"key":"ref_27","first-page":"2032057","article-title":"The effects of secretory IgA in the mucosal immune system","volume":"2020","author":"Li","year":"2020","journal-title":"BioMed Res. Int."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1007\/s12551-020-00698-1","article-title":"Biophysical characterization of dynamic structures of immunoglobulin G","volume":"12","author":"Yanaka","year":"2020","journal-title":"Biophys. Rev."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Zurawski, D.V., and Mclendon, M.K. (2020). Monoclonal antibodies as an antibacterial approach against bacterial pathogens. Antibiotics, 9.","DOI":"10.3390\/antibiotics9040155"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1007\/978-3-319-72077-7_7","article-title":"Anti-bacterial monoclonal antibodies","volume":"1053","author":"Nagy","year":"2017","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1442","DOI":"10.3389\/fimmu.2017.01442","article-title":"Nanobody-based delivery systems for diagnosis and targeted tumor therapy","volume":"8","author":"Hu","year":"2017","journal-title":"Front. Immunol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"e139","DOI":"10.1016\/j.ddtec.2010.03.002","article-title":"Nanobodies-From llamas to therapeutic proteins","volume":"7","author":"Kolkman","year":"2010","journal-title":"Drug Discov. Today Technol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/microbiolspec.AID-0019-2014","article-title":"Functions of antibodies","volume":"2","author":"Forthal","year":"2014","journal-title":"Microbiol. Spectr."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Sawa, T., Kinoshita, M., Inoue, K., Ohara, J., and Moriyama, K. (2019). Immunoglobulin for treating bacterial infections: One more mechanism of action. Antibodies, 8.","DOI":"10.20944\/preprints201909.0144.v1"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1111\/imcb.12324","article-title":"Antibody-mediated complement activation in pathology and protection","volume":"98","author":"Goldberg","year":"2020","journal-title":"Immunol. Cell Biol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1016\/j.ijbiomac.2018.09.054","article-title":"Binding of LcrV protein from Yersinia pestis to human T-cells induces apoptosis, which is completely blocked by specific antibodies","volume":"122","author":"Abramov","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_37","first-page":"505","article-title":"On the origin of the vaccine inoculation","volume":"5","author":"Jenner","year":"1801","journal-title":"Med. Phys. J."},{"key":"ref_38","unstructured":"Morrow, W.J.W., Sheikh, N.A., Schmidt, C.S., and Davies, H.D. (2012). Concept and Scope of Modern Vaccines. Vaccinology: Principles and Practice, Blackwell Publishing Ltd."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"6759","DOI":"10.1016\/j.vaccine.2017.09.070","article-title":"A phase I safety and immunogenicity dose escalation trial of plague vaccine, Flagellin\/F1\/V, in healthy adult volunteers (DMID 08-0066)","volume":"35","author":"Frey","year":"2017","journal-title":"Vaccine"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1002\/lt.20594","article-title":"High dose intravenous immunoglobulin treatment: Mechanisms of action","volume":"11","author":"Boros","year":"2005","journal-title":"Liver Transpl."},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Afonso, A.F.B., and Jo\u00e3o, C.M.P. (2016). The production processes and biological effects of intravenous immunoglobulin. Biomolecules, 6.","DOI":"10.3390\/biom6010015"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1007\/s10875-020-00788-5","article-title":"A systematic review and meta-regression analysis on the impact of increasing IgG trough level on infection rates in primary immunodeficiency patients on intravenous IgG therapy","volume":"40","author":"Lee","year":"2020","journal-title":"J. Clin. Immunol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"S11","DOI":"10.1186\/1710-1492-7-S1-S11","article-title":"Primary immunodeficiency","volume":"7","author":"McCusker","year":"2011","journal-title":"Allergy Asthma Clin. Immunol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.transci.2016.12.017","article-title":"Mechanisms of action of intravenous immunoglobulin","volume":"56","author":"Chaigne","year":"2017","journal-title":"Transfus. Apheresis Sci."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1007\/s10875-007-9088-9","article-title":"Intravenous immunoglobulin: An update on the clinical use and mechanisms of action","volume":"27","author":"Negi","year":"2007","journal-title":"J. Clin. Immunol."},{"key":"ref_46","first-page":"13","article-title":"Use of intravenous and subcutaneous human immunoglobulins","volume":"64","author":"Ramus","year":"2019","journal-title":"Soins Rev. Ref. Infirm."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/j.iac.2015.07.006","article-title":"Immunoglobulin replacement therapy for primary immunodeficiency","volume":"35","author":"Sriaroon","year":"2015","journal-title":"Immunol. Allergy Clin. N. Am."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1097\/MCC.0000000000000639","article-title":"Intravenous immunoglobulin for adjunctive treatment of severe infections in ICUs","volume":"25","author":"Aubron","year":"2019","journal-title":"Curr. Opin. Crit. Care"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1703531","DOI":"10.1080\/19420862.2019.1703531","article-title":"Antibodies to watch in 2020","volume":"12","author":"Kaplon","year":"2020","journal-title":"MAbs"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.jconrel.2019.04.005","article-title":"In a murine model of acute lung infection, airway administration of a therapeutic antibody confers greater protection than parenteral administration","volume":"303","author":"Dalonneau","year":"2019","journal-title":"J. Control Release"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"e00260","DOI":"10.1128\/mSphere.00260-18","article-title":"A novel Shigella proteome microarray discriminates targets of human antibody reactivity following oral vaccination and experimental challenge","volume":"3","author":"Ndungo","year":"2018","journal-title":"Msphere"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"3068","DOI":"10.1128\/IAI.74.5.3068-3070.2006","article-title":"Administration of antibody to the lung protects mice against pneumonic plague","volume":"74","author":"Hill","year":"2006","journal-title":"Infect. Immun."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"e3","DOI":"10.1542\/peds.104.1.e3","article-title":"Early initiation of breastfeeding and the risk of infant diarrhea in rural Egypt","volume":"104","author":"Clemens","year":"1999","journal-title":"Pediatrics"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1093\/infdis\/jiy022","article-title":"Maternal vaccination with a monocomponent pertussis toxoid vaccine is sufficient to protect infants in a baboon model of Whooping cough","volume":"217","author":"Kapil","year":"2018","journal-title":"J. Infect. Dis."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1080\/19420862.2018.1556465","article-title":"Antibodies to watch in 2019","volume":"11","author":"Kaplon","year":"2019","journal-title":"MAbs"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1038\/417584a","article-title":"Magic bullets hit the target","volume":"417","author":"Gura","year":"2002","journal-title":"Nature"},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Hollowell, P., Li, Z., Hu, X., Ruane, S., Kalonia, C., Van der Walle, C.F., and Lu, J.R. (2020). Recent advances in studying interfacial adsorption of bioengineered monoclonal antibodies. Molecules, 25.","DOI":"10.3390\/molecules25092047"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1016\/j.biotechadv.2017.03.011","article-title":"Very-large-scale production of antibodies in plants: The biologization of manufacturing","volume":"35","author":"Buyel","year":"2017","journal-title":"Biotechnol. Adv."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1007\/s10928-014-9367-z","article-title":"Review on modeling anti-antibody responses to monoclonal antibodies","volume":"41","author":"Garrido","year":"2014","journal-title":"J. Pharmacokinet. Pharmacodyn."},{"key":"ref_60","first-page":"220","article-title":"Anti-lipopolysaccharide-immunoglobulin (IgG-Anti-LPS) therapy in intensive care patients following surgery from infectious disease","volume":"17","author":"Wiedeck","year":"1990","journal-title":"Infusiontherapie."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"5880","DOI":"10.4049\/jimmunol.167.10.5880","article-title":"Therapeutic administration of anti-PcrV F(ab\u2032)2 in sepsis associated with Pseudomonas aeruginosa","volume":"167","author":"Shime","year":"2001","journal-title":"J. Immunol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1128\/ecosalplus.esp-0032-2018","article-title":"Fasciano1, Lamyaa Shaban2, and J.M.; Fasciano, A.C.; Shaban, L.; Mecsas, J. Promises and challenges of the type three secretion system- injectisome as an anti-virulence target","volume":"8","author":"Fasciano","year":"2019","journal-title":"EcoSal Plus"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"19","DOI":"10.2174\/187152607780090685","article-title":"Targeting bacterial secretion systems: Benefits of disarmament in the microcosm","volume":"7","author":"Baron","year":"2008","journal-title":"Infect. Disord. Drug Targets"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1016\/S0002-9343(89)80611-4","article-title":"Antibiotic therapy for Pseudomonas aeruginosa bacteremia: Outcome correlations in a prospective study of 200 patients","volume":"87","author":"Hilf","year":"1989","journal-title":"Am. J. Med."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Secher, T., Fas, S., Fauconnier, L., Mathieu, M., Rutschi, O., Ryffel, B., and Rudolf, M. (2013). The anti-Pseudomonas aeruginosa antibody Panobacumab is efficacious on acute pneumonia in neutropenic mice and has additive effects with meropenem. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0073396"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"e00710","DOI":"10.1128\/AAC.00710-19","article-title":"Treatment efficacy of MEDI3902 in Pseudomonas aeruginosa bloodstream infection and acute pneumonia rabbit models","volume":"63","author":"Le","year":"2019","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"3451","DOI":"10.1007\/s00253-016-7388-9","article-title":"Advances in recombinant antibody manufacturing","volume":"100","author":"Kunert","year":"2016","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1002\/bit.25141","article-title":"Cell line profiling to improve monoclonal antibody production","volume":"111","author":"Kang","year":"2014","journal-title":"Biotechnol. Bioeng."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1400","DOI":"10.1002\/btpr.436","article-title":"Maximizing productivity of CHO cell-based fed-batch culture using chemically defined media conditions and typical manufacturing equipment","volume":"26","author":"Huang","year":"2010","journal-title":"Biotechnol. Prog."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1002\/bit.260480205","article-title":"Overexpression of bcl-2, apoptosis suppressing gene: Prolonged viable culture period of hybridoma and enhanced antibody production","volume":"48","author":"Itoh","year":"1995","journal-title":"Biotechnol. Bioeng."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"2531","DOI":"10.1007\/s00253-012-4365-9","article-title":"Overexpression of CHOP alone and in combination with chaperones is effective in improving antibody production in mammalian cells","volume":"97","author":"Nishimiya","year":"2013","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"e100","DOI":"10.14440\/jbm.2018.257","article-title":"Improved production of monoclonal antibodies against the LcrV antigen of Yersinia pestis using FACS-aided hybridoma selection","volume":"5","author":"Sittner","year":"2018","journal-title":"J. Biol. Methods"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1186\/s12934-016-0445-3","article-title":"Enhancing full-length antibody production by signal peptide engineering","volume":"15","author":"Zhou","year":"2016","journal-title":"Microb. Cell Fact."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"270","DOI":"10.3389\/fpls.2019.00270","article-title":"Plant-produced chimeric VHH-sIgA against enterohemorrhagic E. coli intimin shows cross-serotype inhibition of bacterial adhesion to epithelial cells","volume":"10","author":"Saberianfar","year":"2019","journal-title":"Front. Plant Sci."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1007\/s00253-004-1559-9","article-title":"Secretory and extracellular production of recombinant proteins using Escherichia coli","volume":"64","author":"Choi","year":"2004","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Kinoshita, M., Shimizu, M., Akiyama, K., Kato, H., Moriyama, K., and Sawa, T. (2020). Epidemiological survey of serum titers from adults against various Gram-negative bacterial V-antigens. PLoS ONE, 15.","DOI":"10.1371\/journal.pone.0220924"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1001\/jama.1920.26210060004009d","article-title":"The value of bacterial vaccines in immunization and therapy","volume":"74","author":"Moody","year":"1920","journal-title":"J. Am. Med. Assoc."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"S13","DOI":"10.1093\/infdis\/129.Supplement_1.S13","article-title":"Plague immunization. I. Past and present trends","volume":"129","author":"Meyer","year":"1974","journal-title":"J. Infect. Dis."},{"key":"ref_79","first-page":"278","article-title":"The effects of loss of different virulence determinants on the virulence and immunogenicity of strains of Pasteurella pestis","volume":"39","author":"Burrows","year":"1958","journal-title":"Br. J. Exp. Pathol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"179","DOI":"10.4049\/jimmunol.91.2.179","article-title":"Biosynthesis and purification of V and W antigen in Pasteurella pestis","volume":"91","author":"Lawton","year":"1963","journal-title":"J. Immunol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"4192","DOI":"10.1128\/iai.62.10.4192-4201.1994","article-title":"Passive immunity to yersiniae mediated by anti-recombinant V antigen and protein A-V antigen fusion peptide","volume":"62","author":"Motin","year":"1994","journal-title":"Infect. Immun."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1128\/iai.54.2.428-434.1986","article-title":"A low-Ca2+ response operon encodes the V antigen of Yersinia pestis","volume":"54","author":"Perry","year":"1986","journal-title":"Infect. Immun."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/0968-0004(93)90080-7","article-title":"Membrane traffic wardens and protein secretion in Gram-negative bacteria","volume":"18","author":"Salmond","year":"1993","journal-title":"Trends Biochem. Sci."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"6127","DOI":"10.1128\/IAI.73.9.6127-6137.2005","article-title":"Anti-LcrV antibody inhibits delivery of Yops by Yersinia pestis KIM5 by directly promoting phagocytosis","volume":"73","author":"Cowan","year":"2005","journal-title":"Infect. Immun."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"1572","DOI":"10.1128\/IAI.05637-11","article-title":"Polymorphisms in the LcrV gene of Yersinia enterocolitica and their effect on plague protective immunity","volume":"80","author":"Miller","year":"2012","journal-title":"Infect. Immun."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1128\/CVI.00013-14","article-title":"Direct neutralization of type III effector translocation by the variable region of a monoclonal antibody to Yersinia pestis LcrV","volume":"21","author":"Ivanov","year":"2014","journal-title":"Clin. Vaccine Immun."},{"key":"ref_87","doi-asserted-by":"crossref","unstructured":"Xiao, X., Zhu, Z., Dankmeyer, J.L., Wormald, M.M., Fast, R.L., Worsham, P.L., Cote, C.K., Amemiya, K., and Dimitrov, D.S. (2010). Human anti-plague monoclonal antibodies protect mice from Yersinia pestis in a bubonic plague model. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0013047"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1038\/gt.2010.42","article-title":"Affinity maturation of an anti-V antigen IgG expressed in situ through adenovirus gene delivery confers enhanced protection against Yersinia pestis challenge","volume":"17","author":"Ang","year":"2010","journal-title":"Gene Ther."},{"key":"ref_89","doi-asserted-by":"crossref","unstructured":"Zauberman, A., Flashner, Y., Levy, Y., Vagima, Y., Tidhar, A., Cohen, O., Bar-Haim, E., Gur, D., Aftalion, M., and Halperin, G. (2013). YopP-expressing variant of Y. pestis activates a potent innate immune response affording cross-protection against yersiniosis and tularemia. PLoS ONE, 8.","DOI":"10.1371\/annotation\/e6ae3cd6-3d55-4ec6-8437-19572280e260"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1532","DOI":"10.1128\/IAI.73.3.1532-1542.2005","article-title":"Antibody against V antigen prevents Yop-dependent growth of Yersinia pestis","volume":"73","author":"Philipovskiy","year":"2005","journal-title":"Infect. Immun."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1183\/09031936.00147406","article-title":"Effect of anti-PcrV antibody in a murine chronic airway Pseudomonas aeruginosa infection model","volume":"29","author":"Imamura","year":"2007","journal-title":"Eur. Respir. J."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"1837","DOI":"10.1007\/s10096-011-1509-2","article-title":"PcrV antibody-antibiotic combination improves survival in Pseudomonas aeruginosa-infected mice","volume":"31","author":"Song","year":"2012","journal-title":"Eur. J. Clin. Microbiol. Infect. Dis."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/j.molimm.2019.10.005","article-title":"Anti-PcrV IgY antibodies protect against Pseudomonas aeruginosa infection in both acute pneumonia and burn wound models","volume":"116","author":"Ranjbar","year":"2019","journal-title":"Mol. Immunol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1086\/341069","article-title":"Generation and characterization of a protective monoclonal antibody to Pseudomonas aeruginosa PcrV","volume":"186","author":"Frank","year":"2002","journal-title":"J. Infect. Dis."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"15243","DOI":"10.1074\/jbc.M115.684241","article-title":"High throughput combinatorial formatting of PcrV nanobodies for efficient potency improvement","volume":"291","author":"Detalle","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/j.jcf.2017.12.006","article-title":"KB001-A, a novel anti-inflammatory, found to be safe and well-tolerated in cystic fibrosis patients infected with Pseudomonas aeruginosa","volume":"17","author":"Jain","year":"2018","journal-title":"J. Cyst. Fibros."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"4384","DOI":"10.1128\/AAC.02643-14","article-title":"A novel anti-PcrV antibody providing enhanced protection against Pseudomonas aeruginosa in multiple animal infection models","volume":"58","author":"Warrener","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"2843","DOI":"10.4161\/21645515.2014.971641","article-title":"Anti-PcrV antibody strategies against virulent Pseudomonas aeruginosa","volume":"10","author":"Sawa","year":"2014","journal-title":"Hum. Vaccine Immunother."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"e02565","DOI":"10.1128\/AAC.02565-17","article-title":"MEDI3902 correlates of protection against severe Pseudomonas aeruginosa pneumonia in a rabbit acute pneumonia model","volume":"62","author":"Le","year":"2018","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.resp.2014.01.001","article-title":"PcrV antibody protects multi-drug resistant Pseudomonas aeruginosa induced acute lung injury","volume":"193","author":"Wang","year":"2014","journal-title":"Respir. Physiol. Neurobiol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.micpath.2010.02.008","article-title":"Polymorphisms in the Pseudomonas aeruginosa type III secretion protein, PcrV-Implications for anti-PcrV immunotherapy","volume":"48","author":"Lynch","year":"2010","journal-title":"Microb. Pathog."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1016\/0167-5699(95)80008-5","article-title":"IgY: Clues to the origins of modern antibodies","volume":"16","author":"Warr","year":"1995","journal-title":"Immunol. Today"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"2833","DOI":"10.1080\/21645515.2016.1209280","article-title":"The prophylactic effects of human IgG derived from sera containing high anti-PcrV titers against pneumonia-causing Pseudomonas aeruginosa","volume":"12","author":"Kinoshita","year":"2016","journal-title":"Hum. Vaccine Immunother."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"2320","DOI":"10.1097\/CCM.0b013e31825334f6","article-title":"Safety and pharmacokinetics of an anti-PcrV PEGylated monoclonal antibody fragment in mechanically ventilated patients colonized with Pseudomonas aeruginosa: A randomized, double-blind, placebo-controlled trial","volume":"40","author":"Luyt","year":"2012","journal-title":"Crit. Care Med."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1002\/ppul.22890","article-title":"Anti-PcrV antibody in cystic fibrosis: A novel approach targeting Pseudomonas aeruginosa airway infection","volume":"49","author":"Milla","year":"2014","journal-title":"Pediatr. Pulmonol."},{"key":"ref_106","first-page":"1983","article-title":"Pseudomonas aeruginosa PcrV and Psl, the molecular targets of bispecific antibody MEDI3902, are conserved among diverse global clinical isolates","volume":"218","author":"Tabor","year":"2018","journal-title":"J. Infect. Dis."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"e1","DOI":"10.1016\/j.cmi.2018.08.004","article-title":"Phase 1 study of MEDI3902, an investigational anti-Pseudomonas aeruginosa PcrV and Psl bispecific human monoclonal antibody, in healthy adults","volume":"25","author":"Ali","year":"2019","journal-title":"Clin. Microbiol. Infect."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/j.micinf.2005.07.009","article-title":"Recombinant anti-EspA antibodies block Escherichia coli O157:H7-induced attaching and effacing lesions in vitro","volume":"8","author":"Patel","year":"2006","journal-title":"Microbes Infect."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1111\/j.1574-695X.2005.00030.x","article-title":"Use of virulence factor-specific egg yolk-derived immunoglobulins as a promising alternative to antibiotics for prevention of attaching and effacing Escherichia coli infections","volume":"46","author":"Girard","year":"2006","journal-title":"FEMS Immunol. Med. Microbiol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"1206","DOI":"10.1111\/j.1365-2672.2007.03334.x","article-title":"Avian- and mammalian-derived antibodies against adherence-associated proteins inhibit host cell colonization by Escherichia coli O157:H7","volume":"103","author":"Cook","year":"2007","journal-title":"J. Appl. Microbiol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.clim.2010.09.009","article-title":"Identification of a novel linear epitope on EspA from enterohemorrhagic E. coli using a neutralizing and protective monoclonal antibody","volume":"138","author":"Yu","year":"2010","journal-title":"Clin. Immunol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"1595","DOI":"10.1099\/jmm.0.076323-0","article-title":"Monoclonal antibodies against all known variants of EspA: Development of a simple diagnostic test for enteropathogenic Escherichia coli based on a key virulence factor","volume":"63","author":"Praekelt","year":"2014","journal-title":"J. Med. Microbiol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1139\/W10-034","article-title":"Protection of epithelial cells from Salmonella enterica serovar Enteritidis invasion by antibodies against the SPI-1 type III secretion system","volume":"56","author":"Desin","year":"2010","journal-title":"Can. J. Microbiol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1002\/prot.23251","article-title":"Identification of the bile salt binding site on IpaD from Shigella flexneri and the influence of ligand binding on IpaD structure","volume":"80","author":"Barta","year":"2012","journal-title":"Proteins"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"16677","DOI":"10.1074\/jbc.M117.802231","article-title":"Single-domain antibodies pinpoint potential targets within Shigella invasion plasmid antigen D of the needle tip complex for inhibition of type III secretion","volume":"292","author":"Barta","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"5181","DOI":"10.1128\/IAI.00189-08","article-title":"Vaccination of mice with a Yop translocon complex elicits antibodies that are protective against infection with F1\u2212 Yersinia pestis","volume":"76","author":"Ivanov","year":"2008","journal-title":"Infect. Immun."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.vetimm.2012.09.016","article-title":"Antibodies to intimin and Escherichia coli-secreted proteins EspA and EspB in sera of Brazilian children with hemolytic uremic syndrome and healthy controls","volume":"152","author":"Guirro","year":"2013","journal-title":"Vet. Immunol. Immunopathol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"2793","DOI":"10.1016\/j.vaccine.2016.04.056","article-title":"The intranasal vaccination of pregnant dams with Intimin and EspB confers protection in neonatal mice from Escherichia coli (EHEC) O157: H7 infection","volume":"34","author":"Rabinovitz","year":"2016","journal-title":"Vaccine"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"4137","DOI":"10.1128\/IAI.00416-08","article-title":"Inhibition of Salmonella enterica serovar Typhimurium motility and entry into epithelial cells by a protective antilipopolysaccharide monoclonal immunoglobulin A antibody","volume":"76","author":"Forbes","year":"2008","journal-title":"Infect. Immun."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"2454","DOI":"10.1128\/IAI.00018-12","article-title":"Association of a protective monoclonal IgA with the O antigen of Salmonella enterica serovar Typhimurium impacts type 3 secretion and outer membrane integrity","volume":"80","author":"Forbes","year":"2012","journal-title":"Infect. Immun."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/j.pep.2004.11.001","article-title":"Yersinia pestis outer membrane type III secretion protein YscC: Expression, purification, characterization, and induction of specific antiserum","volume":"40","author":"Goodin","year":"2005","journal-title":"Protein Expr. Purif."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1038\/nrmicro3456","article-title":"Secretion systems in Gram-negative bacteria: Structural and mechanistic insights","volume":"13","author":"Costa","year":"2015","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_123","doi-asserted-by":"crossref","unstructured":"Arnoldo, A., Curak, J., Kittanakom, S., Chevelev, I., Lee, V.T., Sahebol-Amri, M., Koscik, B., Ljuma, L., Roy, P.J., and Bedalov, A. (2008). Identification of small molecule inhibitors of Pseudomonas aeruginosa exoenzyme S using a yeast phenotypic screen. PLoS Genet., 4.","DOI":"10.1371\/annotation\/76d35829-07a2-479f-bbc1-cce6755b6d8c"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"1639","DOI":"10.1073\/pnas.1013888108","article-title":"Translocation of surface-localized effectors in type III secretion","volume":"108","author":"Akopyan","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1016\/j.vaccine.2014.01.044","article-title":"A recombinant bivalent fusion protein rVE confers active and passive protection against Yersinia enterocolitica infection in mice","volume":"32","author":"Singh","year":"2014","journal-title":"Vaccine"},{"key":"ref_126","doi-asserted-by":"crossref","unstructured":"Gonz\u00e1lez-Juarbe, N., Shen, H., Bergman, M.A., Orihuela, C.J., and Dube, P.H. (2017). YopE specific CD8+ T cells provide protection against systemic and mucosal Yersinia pseudotuberculosis infection. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0172314"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"4589","DOI":"10.1128\/IAI.72.8.4589-4602.2004","article-title":"The plague virulence protein YopM targets the innate immune response by causing a global depletion of NK cells","volume":"72","author":"Kerschen","year":"2004","journal-title":"Infect. Immun."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1016\/j.ijmm.2014.02.003","article-title":"Rabbit monoclonal antibodies directed at the T3SS effector protein YopM identify human pathogenic Yersinia isolates","volume":"304","author":"Silva","year":"2014","journal-title":"Int. J. Med. Microbiol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"e01003-18","DOI":"10.1128\/mBio.01003-18","article-title":"CRISPR screen reveals that EHEC\u2019s T3SS and Shiga toxin rely on shared host factors for infection","volume":"9","author":"Pacheco","year":"2018","journal-title":"MBio"},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Ruano-Gallego, D., Yara, D.A., Di Ianni, L., Frankel, G., Sch\u00fcller, S., and Fern\u00e1ndez, L.\u00c1. (2019). A nanobody targeting the translocated intimin receptor inhibits the attachment of enterohemorrhagic E. coli to human colonic mucosa. PLoS Pathog., 15.","DOI":"10.1371\/journal.ppat.1008031"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"2966","DOI":"10.1128\/JCM.42.7.2966-2976.2004","article-title":"Isolation of recombinant antibodies against EspA and intimin of Escherichia coli O157:H7","volume":"42","author":"Hawes","year":"2004","journal-title":"J. Clin. Microbiol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"2708","DOI":"10.1128\/IAI.01905-06","article-title":"Systemic CD8 T-cell memory response to a Salmonella pathogenicity island 2 effector is restricted to Salmonella enterica encountered in the gastrointestinal mucosa","volume":"75","author":"McCollister","year":"2007","journal-title":"Infect. Immun."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"6624","DOI":"10.1128\/IAI.68.12.6624-6632.2000","article-title":"Isolation and characterization of a Shigella flexneri invasion complex subunit vaccine","volume":"68","author":"Turbyfill","year":"2000","journal-title":"Infect. Immun."},{"key":"ref_134","doi-asserted-by":"crossref","unstructured":"Desin, T.S., Townsend, H.G., and Potter, A.A. (2015). Antibodies directed against Shiga-toxin producing Escherichia coli serotype O103 type III secreted proteins block adherence of heterologous STEC serotypes to HEp-2 cells. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0139803"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.mib.2008.12.007","article-title":"Role of Pseudomonas aeruginosa type III effectors in disease","volume":"12","author":"Engel","year":"2009","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"3956","DOI":"10.1128\/JCM.43.8.3956-3962.2005","article-title":"Early immune response to the components of the type III system of Pseudomonas aeruginosa in children with cystic fibrosis","volume":"43","author":"Corech","year":"2005","journal-title":"J. Clin. Microbiol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"9969","DOI":"10.1073\/pnas.1101756108","article-title":"Approach to discover T- and B-cell antigens of intracellular pathogens applied to the design of Chlamydia trachomatis vaccines","volume":"108","author":"Finco","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1177\/039463200702000118","article-title":"Human antibody and antigen response to IncA antibody of Chlamydia trachomatis","volume":"20","author":"Tsai","year":"2007","journal-title":"Int. J. Immunopathol. Pharmacol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"4971","DOI":"10.1128\/JB.184.18.4971-4980.2002","article-title":"SpiC is required for translocation of Salmonella pathogenicity island 2 effectors and secretion of translocon proteins SseB and SseC","volume":"184","author":"Freeman","year":"2002","journal-title":"J. Bacteriol."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1089\/mab.2015.0035","article-title":"Preparation of monoclonal antibodies against SpiC protein secreted by T3SS-2 of Salmonella spp.","volume":"34","author":"Geng","year":"2015","journal-title":"Monoclon. Antib. Immunodiagn. Immunother."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1021\/acs.bioconjchem.9b00025","article-title":"Antibody delivery for intracellular targets: Emergent therapeutic potential","volume":"30","author":"Singh","year":"2019","journal-title":"Bioconjugate Chem."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"e01379","DOI":"10.1128\/mBio.01379-14","article-title":"Engineered endolysin-based \u201cArtilysins\u201d to combat multidrug-resistant Gram-negative pathogens","volume":"5","author":"Briers","year":"2014","journal-title":"MBio"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1096\/fj.10-162958","article-title":"Single-domain llama antibodies as specific intracellular inhibitors of SpvB, the actin ADP-ribosylating toxin of Salmonella Typhimurium","volume":"25","author":"Alzogaray","year":"2011","journal-title":"FASEB J."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1099\/0022-1317-50-2-116","article-title":"Type III secretion systems and pathogenicity islands","volume":"50","author":"Winstanley","year":"2001","journal-title":"J. Med. Microbiol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"4882","DOI":"10.1016\/j.jmb.2019.10.026","article-title":"A potent Anti-SpuE antibody allosterically inhibits type III secretion system and attenuates virulence of Pseudomonas aeruginosa","volume":"431","author":"Zhang","year":"2019","journal-title":"J. Mol. Biol."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1111\/1751-7915.13279","article-title":"Immunological blocking of spermidine-mediated host\u2013pathogen communication provides effective control against Pseudomonas aeruginosa infection","volume":"13","author":"Wang","year":"2020","journal-title":"Microb. Biotechnol."}],"container-title":["Antibodies"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4468\/9\/3\/35\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T09:51:55Z","timestamp":1760176315000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4468\/9\/3\/35"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,7,27]]},"references-count":146,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2020,9]]}},"alternative-id":["antib9030035"],"URL":"https:\/\/doi.org\/10.3390\/antib9030035","relation":{},"ISSN":["2073-4468"],"issn-type":[{"value":"2073-4468","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,7,27]]}}}