{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T08:21:21Z","timestamp":1790324481820,"version":"4.1.0"},"reference-count":293,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2022,5,16]],"date-time":"2022-05-16T00:00:00Z","timestamp":1652659200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"The Slovak Research and Development Agency of the Slovak Republic","award":["APVV-17\u20130445 (EV)"],"award-info":[{"award-number":["APVV-17\u20130445 (EV)"]}]},{"name":"The Slovak Research and Development Agency of the Slovak Republic","award":["VEGA No. 2\/0048\/19 (EV)"],"award-info":[{"award-number":["VEGA No. 2\/0048\/19 (EV)"]}]},{"name":"The Slovak Research and Development Agency of the Slovak Republic","award":["VEGA No. 2\/0090\/21 (KT)"],"award-info":[{"award-number":["VEGA No. 2\/0090\/21 (KT)"]}]},{"name":"The Scientific Grant Agency of the Ministry of Education, Science, Research and Sport of Slovak Republic and Slovak Academy of Sciences","award":["APVV-17\u20130445 (EV)"],"award-info":[{"award-number":["APVV-17\u20130445 (EV)"]}]},{"name":"The Scientific Grant Agency of the Ministry of Education, Science, Research and Sport of Slovak Republic and Slovak Academy of Sciences","award":["VEGA No. 2\/0048\/19 (EV)"],"award-info":[{"award-number":["VEGA No. 2\/0048\/19 (EV)"]}]},{"name":"The Scientific Grant Agency of the Ministry of Education, Science, Research and Sport of Slovak Republic and Slovak Academy of Sciences","award":["VEGA No. 2\/0090\/21 (KT)"],"award-info":[{"award-number":["VEGA No. 2\/0090\/21 (KT)"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Viruses"],"abstract":"<jats:p>A severe course of acute respiratory disease caused by influenza A virus (IAV) infection is often linked with subsequent bacterial superinfection, which is difficult to cure. Thus, synergistic influenza\u2013bacterial co-infection represents a serious medical problem. The pathogenic changes in the infected host are accelerated as a consequence of IAV infection, reflecting its impact on the host immune response. IAV infection triggers a complex process linked with the blocking of innate and adaptive immune mechanisms required for effective antiviral defense. Such disbalance of the immune system allows for easier initiation of bacterial superinfection. Therefore, many new studies have emerged that aim to explain why viral\u2013bacterial co-infection can lead to severe respiratory disease with possible fatal outcomes. In this review, we discuss the key role of several IAV proteins\u2014namely, PB1-F2, hemagglutinin (HA), neuraminidase (NA), and NS1\u2014known to play a role in modulating the immune defense of the host, which consequently escalates the development of secondary bacterial infection, most often caused by Streptococcus pneumoniae. Understanding the mechanisms leading to pathological disorders caused by bacterial superinfection after the previous viral infection is important for the development of more effective means of prevention; for example, by vaccination or through therapy using antiviral drugs targeted at critical viral proteins.<\/jats:p>","DOI":"10.3390\/v14051064","type":"journal-article","created":{"date-parts":[[2022,5,16]],"date-time":"2022-05-16T21:36:06Z","timestamp":1652736966000},"page":"1064","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["The Contribution of Viral Proteins to the Synergy of Influenza and Bacterial Co-Infection"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9715-7017","authenticated-orcid":false,"given":"Miriam","family":"Miku\u0161ov\u00e1","sequence":"first","affiliation":[{"name":"Biomedical Research Center of the Slovak Academy of Sciences, Institute of Virology, D\u00fabravsk\u00e1 Cesta 9, 845 05 Bratislava, Slovakia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6988-9352","authenticated-orcid":false,"given":"Karol\u00edna","family":"Tom\u010d\u00edkov\u00e1","sequence":"additional","affiliation":[{"name":"Biomedical Research Center of the Slovak Academy of Sciences, Institute of Virology, D\u00fabravsk\u00e1 Cesta 9, 845 05 Bratislava, Slovakia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0321-3565","authenticated-orcid":false,"given":"Katar\u00edna","family":"Briestensk\u00e1","sequence":"additional","affiliation":[{"name":"Biomedical Research Center of the Slovak Academy of Sciences, Institute of Virology, D\u00fabravsk\u00e1 Cesta 9, 845 05 Bratislava, Slovakia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4304-070X","authenticated-orcid":false,"given":"Franti\u0161ek","family":"Kostolansk\u00fd","sequence":"additional","affiliation":[{"name":"Biomedical Research Center of the Slovak Academy of Sciences, Institute of Virology, D\u00fabravsk\u00e1 Cesta 9, 845 05 Bratislava, Slovakia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6386-651X","authenticated-orcid":false,"given":"Eva","family":"Vare\u010dkov\u00e1","sequence":"additional","affiliation":[{"name":"Biomedical Research Center of the Slovak Academy of Sciences, Institute of Virology, D\u00fabravsk\u00e1 Cesta 9, 845 05 Bratislava, Slovakia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,5,16]]},"reference":[{"key":"ref_1","unstructured":"(2022, April 03). The Top 10 Causes of Death. Available online: https:\/\/www.who.int\/news-room\/fact-sheets\/detail\/the-top-10-causes-of-death."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1097\/MOP.0000000000000712","article-title":"Influenza: Annual seasonal severity","volume":"1","author":"Gavigan","year":"2019","journal-title":"Curr. Opin. Pediatr."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1111\/imr.12692","article-title":"Host-pathogen kinetics during influenza infection and coinfection: Insights from predictive modeling","volume":"285","author":"Smith","year":"2018","journal-title":"Immunol. Rev."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"925","DOI":"10.1089\/jir.2015.0072","article-title":"The Role of Virus Infection in Deregulating the Cytokine Response to Secondary Bacterial Infection","volume":"35","author":"Mehta","year":"2015","journal-title":"J. Interferon Cytokine Res."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/j.ijid.2012.01.003","article-title":"Epidemiology, microbiology, and treatment considerations for bacterial pneumonia complicating influenza","volume":"16","author":"Metersky","year":"2012","journal-title":"Int. J. Infect. Dis."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.3389\/fmicb.2017.01041","article-title":"Secondary Bacterial Infections Associated with Influenza Pandemics","volume":"8","author":"Morris","year":"2017","journal-title":"Front. Microbiol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"338","DOI":"10.3389\/fcimb.2017.00338","article-title":"Mechanisms of Severe Mortality-Associated Bacterial Co-infections Following Influenza Virus Infection","volume":"7","author":"Jia","year":"2017","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1097\/QCO.0000000000000347","article-title":"Bacterial pneumonia as an influenza complication","volume":"30","author":"Schultz","year":"2017","journal-title":"Curr. Opin. Infect. Dis."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2047","DOI":"10.4049\/jimmunol.1301152","article-title":"Immune Dysfunction and Bacterial Co-Infections following Influenza","volume":"191","author":"Metzger","year":"2013","journal-title":"J. Immunol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1448","DOI":"10.1017\/S0950268807000271","article-title":"Invasive pneumococcal and meningococcal disease: Association with influenza virus and respiratory syncytial virus activity?","volume":"136","author":"Jansen","year":"2008","journal-title":"Epidemiol. Infect."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1038\/s41579-018-0001-8","article-title":"Streptococcus pneumoniae: Transmission, colonization and invasion","volume":"16","author":"Weiser","year":"2018","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1001\/jama.2012.194139","article-title":"Bacterial Coinfection in Influenza","volume":"309","author":"Chertow","year":"2013","journal-title":"JAMA"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"4737","DOI":"10.1007\/s00203-021-02458-5","article-title":"Quantification of bacteria by in vivo bioluminescence imaging in comparison with standard spread plate method and reverse transcription quantitative PCR (RT-qPCR)","volume":"203","year":"2021","journal-title":"Arch. Microbiol."},{"key":"ref_14","first-page":"953","article-title":"Disease Severity in Patients with Simultaneous Influenza and Bacterial Pneumonia","volume":"46","author":"Seki","year":"2007","journal-title":"Intern. Med. J."},{"key":"ref_15","unstructured":"(2022, April 03). COVID-19 & Antibiotic Resistance, Available online: https:\/\/www.cdc.gov\/drugresistance\/covid19.html."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"2097","DOI":"10.1002\/iub.2356","article-title":"Bacterial co-infections with SARS-CoV-2","volume":"72","author":"Mirzaei","year":"2020","journal-title":"IUBMB Life"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"643326","DOI":"10.3389\/fcimb.2021.643326","article-title":"Virus-Induced Changes of the Respiratory Tract Environment Promote Secondary Infections With Streptococcus pneumoniae","volume":"11","author":"Sender","year":"2021","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1128\/CMR.00058-05","article-title":"Insights into the Interaction between Influenza Virus and Pneumococcus","volume":"19","author":"McCullers","year":"2006","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"962","DOI":"10.1086\/591708","article-title":"Predominant role of bacterial pneumonia as a cause of death in pandemic influenza: Implications for pandemic influenza preparedness","volume":"198","author":"Morens","year":"2008","journal-title":"J. Infect. Dis."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1007\/s00705-009-0318-8","article-title":"Multiorgan distribution of human influenza A virus strains observed in a mouse model","volume":"154","author":"Mucha","year":"2009","journal-title":"Arch. Virol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/j.coviro.2012.02.013","article-title":"Pathogenesis of influenza virus infections: The good, the bad and the ugly","volume":"2","author":"Kuiken","year":"2012","journal-title":"Curr. Opin. Virol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1055\/s-0036-1584801","article-title":"Human Influenza Virus Infections","volume":"37","author":"Peteranderl","year":"2016","journal-title":"Semin. Respir. Crit. Care Med."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Francis, M.E., King, M.L., and Kelvin, A.A. (2019). Back to the Future for Influenza Preimmunity\u2014Looking Back at Influenza Virus History to Infer the Outcome of Future Infections. Viruses, 11.","DOI":"10.3390\/v11020122"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1007\/s00011-016-0996-0","article-title":"The inflamatory response triggered by Influenza virus: A two edged sword","volume":"66","author":"Tavares","year":"2017","journal-title":"Inflamm. Res."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"320","DOI":"10.3389\/fimmu.2018.00320","article-title":"Host Immune Response to Influenza A Virus Infection","volume":"9","author":"Chen","year":"2018","journal-title":"Front. Immunol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"3","DOI":"10.3389\/fimmu.2020.00003","article-title":"Respiratory Barrier as a Safeguard and Regulator of Defense Against Influenza A Virus and Streptococcus pneumoniae","volume":"11","author":"LeMessurier","year":"2020","journal-title":"Front. Immunol."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Shim, J.M., Kim, J., Tenson, T., Min, J.Y., and Kainov, D.E. (2017). Influenza Virus Infection, Interferon Response, Viral Counter-Response, and Apoptosis. Viruses, 9.","DOI":"10.20944\/preprints201705.0209.v2"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1159\/000508379","article-title":"The Role of Type I IFNs in Influenza: Antiviral Superheroes or Immunopathogenic Villains?","volume":"12","author":"Wu","year":"2020","journal-title":"J. Innate Immun."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"2862","DOI":"10.3389\/fmicb.2019.02862","article-title":"Functional Characterization and Direct Comparison of Influenza A, B, C, and D NS1 Proteins in vitro and in vivo","volume":"10","author":"Nogales","year":"2019","journal-title":"Front. Microbiol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/j.imlet.2011.10.009","article-title":"Potential role for alternatively activated macrophages in the secondary bacterial infection during recovery from influenza","volume":"141","author":"Chen","year":"2012","journal-title":"Immunol. Lett."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1666","DOI":"10.4049\/jimmunol.1002194","article-title":"Influenza A inhibits Th17-mediated host defense against bacterial pneumonia in mice","volume":"186","author":"Kudva","year":"2011","journal-title":"J. Immunol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1910","DOI":"10.1172\/JCI35412","article-title":"Type I IFNs mediate development of postinfluenza bacterial pneumonia in mice","volume":"119","author":"Shahangian","year":"2009","journal-title":"J. Clin. Investig."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"e00506-16","DOI":"10.1128\/mBio.00506-16","article-title":"Differential Type I Interferon Signaling Is a Master Regulator of Susceptibility to Postinfluenza Bacterial Superinfection","volume":"7","author":"Shepardson","year":"2016","journal-title":"MBio"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1097\/INF.0b013e3181cdafc2","article-title":"Viral coinfections in children with invasive pneumococcal disease","volume":"29","author":"Techasaensiri","year":"2010","journal-title":"Pediatr. Infect. Dis. J."},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Hao, W., Wang, L., and Li, S. (2020). Roles of the Non-Structural Proteins of Influenza A Virus. Pathogens, 9.","DOI":"10.3390\/pathogens9100812"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"4816","DOI":"10.1038\/ncomms5816","article-title":"Conserved and host-specific features of influenza virion architecture","volume":"5","author":"Hutchinson","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1940","DOI":"10.1002\/1873-3468.12118","article-title":"Protein-lipid interactions critical to replication of the influenza A virus","volume":"590","author":"Chlanda","year":"2016","journal-title":"FEBS Lett."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"226","DOI":"10.2183\/pjab.88.226","article-title":"Molecular basis of the structure and function of H1 hemagglutinin of influenza virus","volume":"88","author":"Sriwilaijaroen","year":"2012","journal-title":"Proc. Jpn. Acad. Ser. B Phys. Biol. Sci."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1581","DOI":"10.3389\/fimmu.2018.01581","article-title":"Influenza A Virus Cell Entry, Replication, Virion Assembly and Movement","volume":"9","author":"Dou","year":"2018","journal-title":"Front. Immunol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1447","DOI":"10.1016\/j.bpj.2014.02.018","article-title":"pH-Controlled two-step uncoating of influenza virus","volume":"106","author":"Li","year":"2014","journal-title":"Biophys. J."},{"key":"ref_41","first-page":"1151","article-title":"Orthomyxoviridae: The Viruses and Their Replication","volume":"Volume 40","author":"Knipe","year":"2013","journal-title":"Fields Virology"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/j.antiviral.2013.06.005","article-title":"The influenza virus NS1 protein as a therapeutic target","volume":"99","author":"Engel","year":"2013","journal-title":"Antivir. Res."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"2359","DOI":"10.1099\/vir.0.2008\/004606-0","article-title":"The multifunctional NS1 protein of influenza A viruses","volume":"89","author":"Hale","year":"2008","journal-title":"J. Gen. Virol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1128\/JVI.06519-11","article-title":"A second CRM1-dependent nuclear export signal in the influenza A virus NS2 protein contributes to the nuclear export of viral ribonucleoproteins","volume":"87","author":"Huang","year":"2013","journal-title":"J. Virol."},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Paterson, D., and Fodor, E. (2012). Emerging Roles for the Influenza A Virus Nuclear Export Protein (NEP). PLoS Pathog., 8.","DOI":"10.1371\/journal.ppat.1003019"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1038\/s41579-018-0115-z","article-title":"Host and viral determinants of influenza A virus species specificity","volume":"17","author":"Long","year":"2018","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"5274","DOI":"10.3390\/v7102875","article-title":"Modeling Influenza Virus Infection: A Roadmap for Influenza Research","volume":"7","author":"Boianelli","year":"2015","journal-title":"Viruses"},{"key":"ref_48","first-page":"55898","article-title":"Influenza A Virus Studies in a Mouse Model of Infection","volume":"127","author":"Rodriguez","year":"2017","journal-title":"JoVE"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/j.coi.2011.07.016","article-title":"The pathogenesis of influenza virus infections: The contributions of virus and host factors","volume":"23","author":"Fukuyama","year":"2011","journal-title":"Curr. Opin. Immunol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1586\/eri.11.88","article-title":"Pathogenesis of influenza: Virus\u2013host interactions","volume":"9","author":"Godlee","year":"2011","journal-title":"Expert Rev. Anti Infect. Ther."},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Kamal, R.P., Alymova, I.V., and York, I.A. (2017). Evolution and Virulence of Influenza A Virus Protein PB1-F2. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19010096"},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Ko\u0161\u00edk, I., Pr\u00e1znovsk\u00e1, M., Ko\u0161\u00edkov\u00e1, M., Bobi\u0161ov\u00e1, Z., Holl\u00fd, J., Vare\u010dkov\u00e1, E., Kostolansk\u00fd, F., and Russ, G. (2015). The Ubiquitination of the Influenza A Virus PB1-F2 Protein Is Crucial for Its Biological Function. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0118477"},{"key":"ref_53","unstructured":"(2022, April 03). Types of Influenza Viruses, Available online: https:\/\/www.cdc.gov\/flu\/about\/viruses\/types.htm."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.mib.2016.11.003","article-title":"Viral\u2013bacterial co-infections in the respiratory tract","volume":"35","author":"Bakaletz","year":"2017","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2640","DOI":"10.3389\/fimmu.2018.02640","article-title":"Respiratory Viral Infection-Induced Microbiome Alterations and Secondary Bacterial Pneumonia","volume":"9","author":"Hanada","year":"2018","journal-title":"Front. Immunol."},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Kumpitsch, C., Koskinen, K., Sch\u00f6pf, V., and Moissl-Eichinger, C. (2019). The microbiome of the upper respiratory tract in health and disease. BMC Biol., 17.","DOI":"10.1186\/s12915-019-0703-z"},{"key":"ref_57","unstructured":"(2022, April 03). Streptococcus Pneumoniae, Available online: https:\/\/www.cdc.gov\/pneumococcal\/clinicians\/streptococcus-pneumoniae.html."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1366","DOI":"10.3389\/fimmu.2018.01366","article-title":"Streptococcus pneumoniae\u2019s Virulence and Host Immunity: Aging, Diagnostics, and Prevention","volume":"9","author":"Brooks","year":"2018","journal-title":"Front. Immunol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1038\/nrmicro1871","article-title":"The role of Streptococcus pneumoniae virulence factors in host respiratory colonization and disease","volume":"6","author":"Kadioglu","year":"2008","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1128\/microbiolspec.GPP3-0019-2018","article-title":"Streptococcus pneumoniae Capsular Polysaccharide","volume":"7","author":"Paton","year":"2019","journal-title":"Microbiol. Spectr."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"194","DOI":"10.3389\/fcimb.2014.00194","article-title":"Streptococcus pneumoniae biofilm formation and dispersion during colonisation and disease","volume":"4","author":"Chao","year":"2015","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_62","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_63","doi-asserted-by":"crossref","first-page":"e00200-12","DOI":"10.1128\/mBio.00200-12","article-title":"High Levels of Genetic Recombination during Nasopharyngeal Carriage and Biofilm Formation in Streptococcus pneumoniae","volume":"3","author":"Marks","year":"2012","journal-title":"MBio"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.tim.2012.11.005","article-title":"Influence of bacterial interactions on pneumococcal colonization of the nasopharynx","volume":"21","author":"Shak","year":"2013","journal-title":"Trends Microbiol."},{"key":"ref_65","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_66","first-page":"a010215","article-title":"The Pneumococcus: Epidemiology, Microbiology, and Pathogenesis","volume":"3","author":"Tuomanen","year":"2013","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Yau, B., Hunt, N., Mitchell, A., and Too, L. (2018). Blood\u2013Brain Barrier Pathology and CNS Outcomes in Streptococcus pneumoniae Meningitis. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19113555"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"e1562","DOI":"10.1097\/MD.0000000000001562","article-title":"Characteristics and Outcome of Streptococcus pneumoniae Endocarditis in the XXI Century: A Systematic Review of 111 Cases (2000\u20132013)","volume":"94","author":"Valerio","year":"2015","journal-title":"Medicine"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1007\/s40136-017-0152-6","article-title":"Streptococcus pneumoniae Otitis Media Pathogenesis and How It Informs Our Understanding of Vaccine Strategies","volume":"5","author":"Bergenfelz","year":"2017","journal-title":"Curr. Otorhinolaryngol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1001\/jamaoto.2013.1703","article-title":"Orbital complications of acute sinusitis: Changes in the post-pneumococcal vaccine era","volume":"139","author":"Preciado","year":"2013","journal-title":"JAMA Otolaryngol. Head Neck Surg."},{"key":"ref_71","first-page":"938","article-title":"Clinical and Bacteriologic Features of Chronic Sinusitis in Children","volume":"143","author":"Tinkelman","year":"1989","journal-title":"Am. J. Dis. Child."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1093\/clinids\/22.1.100","article-title":"Association of Invasive Pneumococcal Disease with Season, Atmospheric Conditions, Air Pollution, and the Isolation of Respiratory Viruses","volume":"22","author":"Kim","year":"1996","journal-title":"Clin. Infect. Dis."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"C9","DOI":"10.1016\/j.vaccine.2009.06.007","article-title":"Pneumococcal pneumonia and influenza: A deadly combination","volume":"27","author":"Klugman","year":"2009","journal-title":"Vaccine"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1917","DOI":"10.1016\/S0140-6736(11)61051-9","article-title":"Global burden of respiratory infections due to seasonal influenza in young children: A systematic review and meta-analysis","volume":"378","author":"Nair","year":"2011","journal-title":"Lancet"},{"key":"ref_75","first-page":"10-16966","article-title":"Lethal Synergism between Influenza and Streptococcus pneumoniae","volume":"2","author":"Rudd","year":"2016","journal-title":"J. Infect. Pulm. Dis."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"4607","DOI":"10.1128\/IAI.02225-14","article-title":"Dynamic Changes in the Streptococcus pneumoniae Transcriptome during Transition from Biofilm Formation to Invasive Disease upon Influenza A Virus Infection","volume":"82","author":"Pettigrew","year":"2014","journal-title":"Infect. Immun."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1000","DOI":"10.1086\/368163","article-title":"Role of neuraminidase in lethal synergism between influenza virus and Streptococcus pneumoniae","volume":"187","author":"McCullers","year":"2003","journal-title":"J. Infect. Dis."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"105","DOI":"10.3389\/fimmu.2020.00105","article-title":"Inflammation as a Modulator of Host Susceptibility to Pulmonary Influenza, Pneumococcal, and Co-Infections","volume":"11","author":"Aguilera","year":"2020","journal-title":"Front. Immunol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"fnv062","DOI":"10.1093\/femsle\/fnv062","article-title":"Viral bacterial co-infection of the respiratory tract during early childhood","volume":"362","author":"Brealey","year":"2015","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"341","DOI":"10.4049\/jimmunol.1801010","article-title":"Influenza Pathogenesis: The Effect of Host Factors on Severity of Disease","volume":"202","author":"Gounder","year":"2019","journal-title":"J. Immunol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1038\/nrmicro3231","article-title":"The co-pathogenesis of influenza viruses with bacteria in the lung","volume":"12","author":"McCullers","year":"2014","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1528","DOI":"10.1016\/j.ajpath.2014.08.030","article-title":"The Role of Viral, Host, and Secondary Bacterial Factors in Influenza Pathogenesis","volume":"185","author":"Kash","year":"2015","journal-title":"Am. J. Pathol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1196","DOI":"10.1111\/j.1365-2958.2006.05310.x","article-title":"Switch from planktonic to sessile life: A major event in pneumococcal pathogenesis","volume":"61","author":"Oggioni","year":"2006","journal-title":"Mol. Microbiol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1016\/j.virusres.2011.09.003","article-title":"Insights on influenza pathogenesis from the grave","volume":"162","author":"Taubenberger","year":"2011","journal-title":"Virus Res."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1165\/rcmb.2007-0417OC","article-title":"Influenza Virus Infection Decreases Tracheal Mucociliary Velocity and Clearance of Streptococcus pneumoniae","volume":"42","author":"Pittet","year":"2010","journal-title":"Am. J. Respir. Cell Mol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1111\/j.1469-0691.2007.01910.x","article-title":"Reducing antibiotic use in influenza: Challenges and rewards","volume":"14","author":"Low","year":"2008","journal-title":"Clin. Microbiol. Infect."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"e00438-13","DOI":"10.1128\/mBio.00438-13","article-title":"Interkingdom Signaling Induces Streptococcus pneumoniae Biofilm Dispersion and Transition from Asymptomatic Colonization to Disease","volume":"4","author":"Marks","year":"2013","journal-title":"MBio"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"6707","DOI":"10.1128\/IAI.00789-06","article-title":"Both Influenza-Induced Neutrophil Dysfunction and Neutrophil-Independent Mechanisms Contribute to Increased Susceptibility to a Secondary Streptococcus pneumoniae Infection","volume":"74","author":"McNamee","year":"2006","journal-title":"Infect. Immun."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1089\/jir.2010.0049","article-title":"Postinfluenza bacterial pneumonia: Host defenses gone awry","volume":"30","author":"Ballinger","year":"2010","journal-title":"J. Interferon Cytokine Res."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.4049\/jimmunol.1300014","article-title":"Depletion of alveolar macrophages during influenza infection facilitates bacterial superinfections","volume":"191","author":"Ghoneim","year":"2013","journal-title":"J. Immunol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"846","DOI":"10.1038\/s41467-017-00928-3","article-title":"Alveolar macrophages are critical for broadly-reactive antibody-mediated protection against influenza A virus in mice","volume":"8","author":"He","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"847","DOI":"10.2217\/fvl.14.65","article-title":"The role of macrophages in influenza A virus infection","volume":"9","author":"Nicol","year":"2014","journal-title":"Future Virol."},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Wilden, J.J., Jacob, J.C., Ehrhardt, C., Ludwig, S., and Boergeling, Y. (2021). Altered Signal Transduction in the Immune Response to Influenza Virus and S. pneumoniae or S. aureus Co-Infections. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22115486"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/S0166-0934(01)00287-7","article-title":"Decreased pulmonary clearance of S. pneumoniae following influenza A infection in mice","volume":"94","author":"LeVine","year":"2001","journal-title":"J. Virol. Methods"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1086\/341462","article-title":"Lethal synergism between influenza virus and Streptococcus pneumoniae: Characterization of a mouse model and the role of platelet-activating factor receptor","volume":"186","author":"McCullers","year":"2002","journal-title":"J. Infect. Dis."},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Smith, A.M., Adler, F.R., Ribeiro, R.M., Gutenkunst, R.N., McAuley, J.L., McCullers, J.A., and Perelson, A.S. (2013). Kinetics of coinfection with influenza A virus and Streptococcus pneumoniae. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003238"},{"key":"ref_97","first-page":"327","article-title":"Secondary Bacterial Infections in Influenza Virus Infection Pathogenesis","volume":"Volume 385","author":"Compans","year":"2014","journal-title":"Influenza Pathogenesis and Control\u2014Volume I. Current Topics in Microbiology and Immunology"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.coi.2015.02.002","article-title":"The immunology of influenza virus-associated bacterial pneumonia","volume":"34","author":"Robinson","year":"2015","journal-title":"Curr. Opin. Immunol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1084\/jem.20070891","article-title":"Sustained desensitization to bacterial Toll-like receptor ligands after resolution of respiratory influenza infection","volume":"205","author":"Didierlaurent","year":"2008","journal-title":"J. Exp. Med."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"1074","DOI":"10.1038\/ni.1637","article-title":"A critical function for CD200 in lung immune homeostasis and the severity of influenza infection","volume":"9","author":"Snelgrove","year":"2008","journal-title":"Nat. Immunol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"12304","DOI":"10.1128\/JVI.01269-12","article-title":"Type I interferon induction during influenza virus infection increases susceptibility to secondary Streptococcus pneumoniae infection by negative regulation of \u03b3\u03b4 T cells","volume":"86","author":"Li","year":"2012","journal-title":"J. Virol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1038\/nm1765","article-title":"Inhibition of pulmonary antibacterial defense by interferon-gamma during recovery from influenza infection","volume":"14","author":"Sun","year":"2008","journal-title":"Nat. Med."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1038\/s41385-019-0158-0","article-title":"Regulatory cytokine function in the respiratory tract","volume":"12","author":"Branchett","year":"2019","journal-title":"Mucosal Immunol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1038\/nm.1929","article-title":"Effector T cells control lung inflammation during acute influenza virus infection by producing IL-10","volume":"15","author":"Sun","year":"2009","journal-title":"Nat. Med."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"550","DOI":"10.3389\/fimmu.2017.00550","article-title":"A Role for Neutrophils in Viral Respiratory Disease","volume":"8","author":"Camp","year":"2017","journal-title":"Front. Immunol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"2395","DOI":"10.1182\/blood.V93.7.2395","article-title":"Influenza A virus accelerates neutrophil apoptosis and markedly potentiates apoptotic effects of bacteria","volume":"93","author":"Colamussi","year":"1999","journal-title":"Blood"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1189\/jlb.3A0614-313RRR","article-title":"Ion efflux and influenza infection trigger NLRP3 inflammasome signaling in human dendritic cells","volume":"99","author":"Fernandez","year":"2016","journal-title":"J. Leukoc. Biol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1007\/s12250-016-3918-y","article-title":"Avian influenza virus directly infects human natural killer cells and inhibits cell activity","volume":"32","author":"Mao","year":"2017","journal-title":"Virol. Sin."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"425","DOI":"10.3389\/fcimb.2020.00425","article-title":"Dynamic Natural Killer Cell and T Cell Responses to Influenza Infection","volume":"10","author":"Frank","year":"2020","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1038\/cmi.2017.10","article-title":"Uncompromised NK cell activation is essential for virus-specific CTL activity during acute influenza virus infection","volume":"15","author":"Liu","year":"2018","journal-title":"Cell. Mol. Immunol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1690","DOI":"10.1093\/infdis\/jiv261","article-title":"Viral Interference: The Case of Influenza Viruses","volume":"212","year":"2015","journal-title":"J. Infect. Dis."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"2048","DOI":"10.4049\/jimmunol.0902772","article-title":"Influenza infection leads to increased susceptibility to subsequent bacterial superinfection by impairing NK cell responses in the lung","volume":"184","author":"Small","year":"2010","journal-title":"J. Immunol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"3667","DOI":"10.1128\/jvi.68.6.3667-3673.1994","article-title":"Apoptosis: A mechanism of cell killing by influenza A and B viruses","volume":"68","author":"Hinshaw","year":"1994","journal-title":"J. Virol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1080\/21505594.2019.1605803","article-title":"The roles of apoptosis, autophagy and unfolded protein response in arbovirus, influenza virus, and HIV infections","volume":"10","author":"Mehrbod","year":"2019","journal-title":"Virulence"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1099\/0022-1317-80-1-137","article-title":"Role of neuraminidase in influenza virus-induced apoptosis","volume":"80","author":"Morris","year":"1999","journal-title":"J. Gen. Virol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1080\/21505594.2021.2014680","article-title":"The battle for autophagy between host and influenza A virus","volume":"13","author":"Zhou","year":"2021","journal-title":"Virulence"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1002","DOI":"10.1038\/s41419-018-1035-6","article-title":"The induction and consequences of Influenza A virus-induced cell death","volume":"9","author":"Duan","year":"2018","journal-title":"Cell Death Dis."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"3801026","DOI":"10.1155\/2016\/3801026","article-title":"Role of Autophagy and Apoptosis in the Postinfluenza Bacterial Pneumonia","volume":"2016","author":"Qin","year":"2016","journal-title":"Biomed. Res. Int."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"13107","DOI":"10.1128\/JVI.02148-13","article-title":"Influenza A virus proteins NS1 and hemagglutinin along with M2 are involved in stimulation of autophagy in infected cells","volume":"87","author":"Zhirnov","year":"2013","journal-title":"J. Virol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1617","DOI":"10.1128\/JVI.76.4.1617-1625.2002","article-title":"NS1 protein of influenza A virus down-regulates apoptosis","volume":"76","author":"Zhirnov","year":"2002","journal-title":"J. Virol."},{"key":"ref_121","first-page":"20","article-title":"Role for autophagy in cellular response to influenza virus infection","volume":"20","author":"Law","year":"2014","journal-title":"Hong Kong Med. J."},{"key":"ref_122","first-page":"654","article-title":"Networks of Host Factors that Interact with NS1 Protein of Influenza A Virus","volume":"7","author":"Zhou","year":"2016","journal-title":"Front. Microbiol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.coviro.2011.05.016","article-title":"Autophagy in the control and pathogenesis of viral infection","volume":"1","author":"Yordy","year":"2011","journal-title":"Curr. Opin. Virol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"321","DOI":"10.4161\/auto.5.3.7406","article-title":"Autophagy is involved in influenza A virus replication","volume":"5","author":"Zhou","year":"2009","journal-title":"Autophagy"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"554","DOI":"10.1186\/1743-422X-8-554","article-title":"Apoptosis, cytokine and chemokine induction by non-structural 1 (NS1) proteins encoded by different influenza subtypes","volume":"8","author":"Lam","year":"2011","journal-title":"Virol. J."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1016\/j.jgg.2011.10.002","article-title":"Avian influenza A virus H5N1 causes autophagy-mediated cell death through suppression of mTOR signaling","volume":"38","author":"Ma","year":"2011","journal-title":"J. Genet. Genom."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"ra16","DOI":"10.1126\/scisignal.2001931","article-title":"Inhibition of autophagy ameliorates acute lung injury caused by avian influenza A H5N1 infection","volume":"5","author":"Sun","year":"2012","journal-title":"Sci. Signal."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"e01984-18","DOI":"10.1128\/JVI.01984-18","article-title":"Autophagy Promotes Replication of Influenza A Virus In Vitro","volume":"93","author":"Wang","year":"2019","journal-title":"J. Virol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1016\/j.chom.2009.09.005","article-title":"Matrix protein 2 of influenza A virus blocks autophagosome fusion with lysosomes","volume":"6","author":"Dormann","year":"2009","journal-title":"Cell Host Microbe"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1189\/jlb.1011530","article-title":"Apoptosis signaling in influenza virus propagation, innate host defense, and lung injury","volume":"92","author":"Herold","year":"2012","journal-title":"J. Leukoc. Biol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/j.bbrc.2013.10.100","article-title":"Relevance of signaling molecules for apoptosis induction on influenza A virus replication","volume":"441","author":"Iwai","year":"2013","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"7875","DOI":"10.1128\/JVI.75.17.7875-7881.2001","article-title":"Influenza Virus Ns1 Protein Induces Apoptosis in Cultured Cells","volume":"75","author":"Neumann","year":"2001","journal-title":"J. Virol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"1306","DOI":"10.1038\/nm1201-1306","article-title":"A novel influenza A virus mitochondrial protein that induces cell death","volume":"7","author":"Chen","year":"2001","journal-title":"Nat. Med."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1016\/j.bbamcr.2017.10.014","article-title":"Autophagy activation is required for influenza A virus-induced apoptosis and replication","volume":"1865","author":"Yeganeh","year":"2018","journal-title":"Biochim. Biophys. Acta\u2014Mol. Cell Res."},{"key":"ref_135","first-page":"498083","article-title":"The regulation of autophagy by influenza A virus","volume":"2014","author":"Zhang","year":"2014","journal-title":"Biomed. Res. Int."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"451","DOI":"10.7883\/yoken.64.451","article-title":"Increase of apoptosis in a murine model for severe pneumococcal pneumonia during influenza A virus infection","volume":"64","author":"Kosai","year":"2011","journal-title":"Jpn. J. Infect. Dis."},{"key":"ref_137","first-page":"33","article-title":"Why is coinfection with influenza virus and bacteria so difficult to control?","volume":"19","author":"Cauley","year":"2015","journal-title":"Discov. Med."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"4828","DOI":"10.4049\/jimmunol.1202673","article-title":"Neuraminidase reprograms lung tissue and potentiates lipopolysaccharide-induced acute lung injury in mice","volume":"191","author":"Feng","year":"2013","journal-title":"J. Immunol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.chom.2014.06.005","article-title":"Influenza promotes pneumococcal growth during coinfection by providing host sialylated substrates as a nutrient source","volume":"16","author":"Siegel","year":"2014","journal-title":"Cell Host Microbe"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"10557","DOI":"10.1128\/JVI.00330-09","article-title":"The NS1 protein of the 1918 pandemic influenza virus blocks host interferon and lipid metabolism pathways","volume":"83","author":"Billharz","year":"2009","journal-title":"J Virol."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"670177","DOI":"10.3389\/fcimb.2021.670177","article-title":"NS1: A Key Protein in the \u201cGame\u201d Between Influenza A Virus and Host in Innate Immunity","volume":"11","author":"Ji","year":"2021","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"e197","DOI":"10.1038\/cddis.2011.75","article-title":"Cell death regulation during influenza A virus infection by matrix (M1) protein: A model of viral control over the cellular survival pathway","volume":"2","author":"Halder","year":"2011","journal-title":"Cell Death Dis."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"e2018","DOI":"10.1038\/cddis.2015.360","article-title":"Nucleoprotein of influenza A virus negatively impacts antiapoptotic protein API5 to enhance E2F1-dependent apoptosis and virus replication","volume":"6","author":"Mayank","year":"2015","journal-title":"Cell Death Dis."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1038\/cddis.2013.89","article-title":"Influenza A virus nucleoprotein induces apoptosis in human airway epithelial cells: Implications of a novel interaction between nucleoprotein and host protein Clusterin","volume":"4","author":"Tripathi","year":"2013","journal-title":"Cell Death Dis."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1038\/ni.1861","article-title":"Influenza virus activates inflammasomes via its intracellular M2 ion channel","volume":"11","author":"Ichinohe","year":"2010","journal-title":"Nat. Immunol."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"763","DOI":"10.1002\/JLB.4MR0320-206R","article-title":"Influenza A virus PB1-F2 protein: An ambivalent innate immune modulator and virulence factor","volume":"107","author":"Cheung","year":"2020","journal-title":"J. Leukoc. Biol."},{"key":"ref_147","doi-asserted-by":"crossref","unstructured":"Laghlali, G., Lawlor, K.E., and Tate, M.D. (2020). Die Another Way: Interplay between Influenza A Virus, Inflammation and Cell Death. Viruses, 12.","DOI":"10.3390\/v12040401"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"652","DOI":"10.1128\/JVI.01987-10","article-title":"A single N66S mutation in the PB1-F2 protein of influenza A virus increases virulence by inhibiting the early interferon response in vivo","volume":"85","author":"Conenello","year":"2011","journal-title":"J. Virol."},{"key":"ref_149","doi-asserted-by":"crossref","unstructured":"Varga, Z.T., Ramos, I., Hai, R., Schmolke, M., Garc\u00eda-Sastre, A., Fernandez-Sesma, A., and Palese, P. (2011). The influenza virus protein PB1-F2 inhibits the induction of type I interferon at the level of the MAVS adaptor protein. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1002067"},{"key":"ref_150","doi-asserted-by":"crossref","unstructured":"Zamarin, D., Garcia-Sastre, A., Xiao, X., Wang, R., and Palese, P. (2005). Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1. PLoS Pathog., 1.","DOI":"10.1371\/journal.ppat.0010004"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1080\/15548627.2020.1725375","article-title":"Influenza A virus protein PB1-F2 impairs innate immunity by inducing mitophagy","volume":"17","author":"Wang","year":"2021","journal-title":"Autophagy"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1128\/JVI.01373-13","article-title":"A novel cytotoxic sequence contributes to influenza A viral protein PB1-F2 pathogenicity and predisposition to secondary bacterial infection","volume":"88","author":"Alymova","year":"2014","journal-title":"J. Virol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"12324","DOI":"10.1128\/JVI.05872-11","article-title":"Immunopathogenic and antibacterial effects of H3N2 influenza A virus PB1-F2 map to amino acid residues 62, 75, 79, and 82","volume":"85","author":"Alymova","year":"2011","journal-title":"J. Virol."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1186\/s12985-017-0827-0","article-title":"Rapid evolution of the PB1-F2 virulence protein expressed by human seasonal H3N2 influenza viruses reduces inflammatory responses to infection","volume":"14","author":"McAuley","year":"2017","journal-title":"Virol. J."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"1414","DOI":"10.1371\/journal.ppat.0030141","article-title":"A single mutation in the PB1-F2 of H5N1 (HK\/97) and 1918 influenza A viruses contributes to increased virulence","volume":"3","author":"Conenello","year":"2007","journal-title":"PLoS Pathog."},{"key":"ref_156","doi-asserted-by":"crossref","unstructured":"McAuley, J.L., Tate, M.D., MacKenzie-Kludas, C.J., Pinar, A., Zeng, W., Stutz, A., Latz, E., Brown, L.E., and Mansell, A. (2013). Activation of the NLRP3 inflammasome by IAV virulence protein PB1-F2 contributes to severe pathophysiology and disease. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003392"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1074\/jbc.M116.756379","article-title":"PB1-F2 Peptide Derived from Avian Influenza A Virus H7N9 Induces Inflammation via Activation of the NLRP3 Inflammasome","volume":"292","author":"Pinar","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"4713","DOI":"10.1038\/ncomms5713","article-title":"Influenza A virus protein PB1-F2 translocates into mitochondria via Tom40 channels and impairs innate immunity","volume":"5","author":"Yoshizumi","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"566348","DOI":"10.3389\/fmicb.2020.566348","article-title":"Influenza A Virus Induces Autophagy By Its Hemagglutinin Binding To Cell Surface Heat Shock Protein 90aa1","volume":"11","author":"Wang","year":"2020","journal-title":"Front. Microbiol."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1089\/vim.2017.0193","article-title":"Contributions of Influenza Virus Hemagglutinin and Host Immune Responses Toward the Severity of Influenza Virus: Streptococcus pyogenes Superinfections","volume":"31","author":"Klonoski","year":"2018","journal-title":"Viral immunol."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.molimm.2014.12.010","article-title":"Desialylation of airway epithelial cells during influenza virus infection enhances pneumococcal adhesion via galectin binding","volume":"65","author":"Banerjee","year":"2015","journal-title":"Mol. Immunol."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/j.molimm.2015.08.005","article-title":"Galectins regulate the inflammatory response in airway epithelial cells exposed to microbial neuraminidase by modulating the expression of SOCS1 and RIG1","volume":"68","author":"Banerjee","year":"2015","journal-title":"Mol. Immunol."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1016\/S0966-842X(99)01498-5","article-title":"Transforming growth factor beta in infectious disease: Always there for the host and the pathogen","volume":"7","author":"Fitzpatrick","year":"1999","journal-title":"Trends Microbiol."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1073\/pnas.1414422112","article-title":"Influenza viral neuraminidase primes bacterial coinfection through TGF-\u03b2-mediated expression of host cell receptors","volume":"112","author":"Li","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"6374","DOI":"10.1038\/ncomms7374","article-title":"IL-10 inhibits neuraminidase-activated TGF-\u03b2 and facilitates Th1 phenotype during early phase of infection","volume":"6","author":"Dutta","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/j.chom.2009.04.006","article-title":"Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I","volume":"5","author":"Gack","year":"2009","journal-title":"Cell Host Microbe"},{"key":"ref_167","doi-asserted-by":"crossref","unstructured":"Rajsbaum, R., Albrecht, R.A., Wang, M.K., Maharaj, N.P., Versteeg, G.A., Nistal-Vill\u00e1n, E., Garc\u00eda-Sastre, A., and Gack, M.U. (2012). Species-specific inhibition of RIG-I ubiquitination and IFN induction by the influenza A virus NS1 protein. PLoS Pathog., 8.","DOI":"10.1371\/journal.ppat.1003059"},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"3325","DOI":"10.1099\/0022-1317-73-12-3325","article-title":"Binding of influenza A virus NS1 protein to dsRNA in vitro","volume":"73","author":"Hatada","year":"1992","journal-title":"J. Gen. Virol."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"2425","DOI":"10.1128\/JVI.73.3.2425-2433.1999","article-title":"Mutant influenza viruses with a defective NS1 protein cannot block the activation of PKR in infected cells","volume":"73","author":"Hatada","year":"1999","journal-title":"J. Virol."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"6203","DOI":"10.1128\/JVI.74.13.6203-6206.2000","article-title":"Influenza virus NS1 protein counteracts PKR-mediated inhibition of replication","volume":"74","author":"Bergmann","year":"2000","journal-title":"J. Virol."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/j.virol.2007.01.038","article-title":"A Site on the Influenza A Virus NS1 Protein Mediates Both Inhibition of PKR Activation and Temporal Regulation of Viral RNA Synthesis","volume":"363","author":"Min","year":"2007","journal-title":"Virology"},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"7100","DOI":"10.1073\/pnas.0602184103","article-title":"The primary function of RNA binding by the influenza A virus NS1 protein in infected cells: Inhibiting the 2\u2032-5\u2032 oligo (A) synthe-tase\/RNase L pathway","volume":"103","author":"Min","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"7989","DOI":"10.1128\/JVI.74.17.7989-7996.2000","article-title":"Activation of Interferon Regulatory Factor 3 Is Inhibited by the Influenza A Virus NS1 Protein","volume":"74","author":"Talon","year":"2000","journal-title":"J. Virol."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"779","DOI":"10.3389\/fimmu.2017.00779","article-title":"The C-Terminal Effector Domain of Non-Structural Protein 1 of Influenza A Virus Blocks IFN-\u03b2 Production by Targeting TNF Receptor-Associated Factor 3","volume":"8","author":"Qian","year":"2017","journal-title":"Front. Immunol."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1016\/j.bbrc.2016.11.166","article-title":"Influenza a virus NS1 protein induced A20 contributes to viral replication by suppressing interferon-induced antiviral response","volume":"482","author":"Feng","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"4381","DOI":"10.1073\/pnas.0800482105","article-title":"A new influenza virus virulence determinant: The NS1 protein four C-terminal residues modulate pathogenicity","volume":"105","author":"Jackson","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"14194","DOI":"10.1073\/pnas.0606109103","article-title":"Influenza A virus NS1 protein binds p85beta and activates phosphatidylinositol-3-kinase signaling","volume":"103","author":"Hale","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1099\/vir.0.82419-0","article-title":"Influenza A virus NS1 protein activates the phosphatidylinositol 3-kinase (PI3K)\/Akt pathway by direct interaction with the p85 subunit of PI3K","volume":"88","author":"Shin","year":"2007","journal-title":"J. Gen. Virol."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"12730","DOI":"10.1128\/JVI.01427-07","article-title":"SH3 binding motif 1 in influenza A virus NS1 protein is essential for PI3K\/Akt signaling pathway activation","volume":"81","author":"Shin","year":"2007","journal-title":"J. Virol."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1186\/1743-422X-9-149","article-title":"Non Structural Protein of Avian Influenza A (H11N1) Virus Is a Weaker Suppressor of Immune Responses But Capable of Inducing Apoptosis in Host Cells","volume":"9","author":"Mukherjee","year":"2012","journal-title":"Virol. J."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1186\/1743-422X-8-181","article-title":"The NS1 protein of influenza A virus interacts with heat shock protein Hsp90 in human alveolar basal epithelial cells: Implication for virus-induced apoptosis","volume":"8","author":"Zhang","year":"2011","journal-title":"Virol. J."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/j.bbrc.2010.03.160","article-title":"The non-Structural (NS1) Protein of Influenza A Virus Associates With p53 and Inhibits p53-mediated Transcriptional Activity and Apoptosis","volume":"395","author":"Wang","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"17761","DOI":"10.1038\/s41598-017-18087-2","article-title":"Non-structural protein 1 of H3N2 influenza A virus induces nucleolar stress via interaction with nucleolin","volume":"7","author":"Yan","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"1419","DOI":"10.1007\/s10495-007-0071-y","article-title":"Control of apoptosis in influenza virus-infected cells by up-regulation of Akt and p53 signaling","volume":"12","author":"Zhirnov","year":"2007","journal-title":"Apoptosis"},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.1038\/s41564-021-00964-2","article-title":"Restriction factor compendium for influenza A virus reveals a mechanism for evasion of autophagy","volume":"6","author":"Tripathi","year":"2021","journal-title":"Nat. Microbiol."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/j.chom.2014.01.006","article-title":"A LC3-interacting motif in the influenza A virus M2 protein is required to subvert autophagy and maintain virion stability","volume":"15","author":"Beale","year":"2014","journal-title":"Cell Host Microbe"},{"key":"ref_187","doi-asserted-by":"crossref","unstructured":"Alymova, I.V., York, I.A., and McCullers, J.A. (2014). Non-avian animal reservoirs present a source of influenza A PB1-F2 proteins with novel virulence-enhancing markers. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0111603"},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"7474","DOI":"10.1038\/s41598-018-25707-y","article-title":"Virulent PB1-F2 residues: Effects on fitness of H1N1 influenza A virus in mice and changes during evolution of human influenza A viruses","volume":"8","author":"Alymova","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1074\/jbc.M606494200","article-title":"Structural characterization and oligomerization of PB1-F2, a proapoptotic influenza A virus protein","volume":"282","author":"Bruns","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"13233","DOI":"10.1074\/jbc.M109.067710","article-title":"PB1-F2 influenza A virus protein adopts a beta-sheet conformation and forms amyloid fibers in membrane environments","volume":"285","author":"Chevalier","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1002\/psc.641","article-title":"Influenza A virus protein PB1-F2: Synthesis and characterization of the biologically active full length protein and related peptides","volume":"11","author":"Henklein","year":"2005","journal-title":"J. Peptide Sci."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1111\/j.1462-5822.2008.01116.x","article-title":"The proapoptotic influenza A virus protein PB1-F2 regulates viral polymerase activity by interaction with the PB1 protein","volume":"10","author":"Mazur","year":"2008","journal-title":"Cell. Microbiol."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"10051","DOI":"10.1128\/JVI.00592-10","article-title":"Differential localization and function of PB1-F2 derived from different strains of influenza A virus","volume":"84","author":"Chen","year":"2010","journal-title":"J. Virol."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"45","DOI":"10.4149\/av_2011_01_45","article-title":"N-terminal region of the PB1-F2 protein is responsible for increased expression of influenza a viral protein PB1","volume":"55","author":"Kosik","year":"2011","journal-title":"Acta Virol."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.virol.2013.02.025","article-title":"An insight into the PB1F2 protein and its multifunctional role in enhancing the pathogenicity of the influenza A viruses","volume":"440","author":"Chakrabarti","year":"2013","journal-title":"Virology"},{"key":"ref_196","doi-asserted-by":"crossref","unstructured":"Smith, A.M., Adler, F.R., McAuley, J.L., Gutenkunst, R.N., Ribeiro, R.M., McCullers, J.A., and Perelson, A.S. (2011). Effect of 1918 pb1-f2 expression on influenza a virus infection kinetics. PLoS Comput. Biol., 7.","DOI":"10.1371\/journal.pcbi.1001081"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1186\/1743-422X-4-9","article-title":"The PB1-F2 protein of Influenza A virus: Increasing pathogenicity by disrupting alveolar macrophages","volume":"4","author":"Coleman","year":"2007","journal-title":"Virol. J."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1038\/icb.2015.115","article-title":"Induction of memory cytotoxic T cells to influenza A virus and subsequent viral clearance is not modulated by PB1-F2-dependent inflammasome activation","volume":"94","author":"Lee","year":"2016","journal-title":"Immunol. Cell. Biol."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"7214","DOI":"10.1128\/JVI.77.13.7214-7224.2003","article-title":"The Influenza A Virus PB1-F2 Protein Targets the Inner Mitochondrial Membrane via a Predicted Basic Amphipathic Helix That Disrupts Mitochondrial Function","volume":"77","author":"Gibbs","year":"2003","journal-title":"J. Virol."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/j.febslet.2004.11.017","article-title":"Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria","volume":"578","author":"Yamada","year":"2004","journal-title":"FEBS Lett."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"542","DOI":"10.4161\/viru.2.6.17812","article-title":"The influenza A virus protein PB1-F2","volume":"2","author":"Varga","year":"2011","journal-title":"Virulence"},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1016\/j.chom.2007.09.001","article-title":"Expression of the 1918 influenza A virus PB1-F2 enhances the pathogenesis of viral and secondary bacterial pneumonia","volume":"2","author":"McAuley","year":"2007","journal-title":"Cell Host Microbe"},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"9035","DOI":"10.1128\/JVI.00369-12","article-title":"Naturally occurring swine influenza A virus PB1-F2 phenotypes that contribute to superinfection with Gram-positive respiratory pathogens","volume":"86","author":"Hurtig","year":"2012","journal-title":"J. Virol."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.coi.2018.06.005","article-title":"An update on the NLRP3 inflammasome and influenza: The road to redemption or perdition?","volume":"54","author":"Tate","year":"2018","journal-title":"Curr. Opin. Immunol."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"211","DOI":"10.3389\/fimmu.2020.00211","article-title":"NLRP3Inflammasome\u2014A Key Player in Antiviral Responses","volume":"11","author":"Zhao","year":"2020","journal-title":"Front. Immunol."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1111\/j.1600-065X.2011.01041.x","article-title":"Molecular mechanisms of inflammasome activation during microbial infections","volume":"243","author":"Broz","year":"2011","journal-title":"Immunol. Rev."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1016\/j.immuni.2009.02.005","article-title":"The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA","volume":"30","author":"Allen","year":"2009","journal-title":"Immunity"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/j.immuni.2011.02.006","article-title":"Type I interferon inhibits interleukin-1 production and inflammasome activation","volume":"34","author":"Guarda","year":"2011","journal-title":"Immunity"},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"568","DOI":"10.1016\/j.bbapap.2012.11.009","article-title":"Influenza A virus protein PB1-F2 from different strains shows distinct structural signatures","volume":"1834","author":"Solbak","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"138","DOI":"10.4149\/av_2013_02_138","article-title":"PB1-F2 expedition from the whole protein through the domain to aa residue function","volume":"57","author":"Russ","year":"2013","journal-title":"Acta Virol."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1186\/1743-422X-7-351","article-title":"Conserved epitopes of influenza A virus inducing protective immunity and their prospects for universal vaccine development","volume":"7","year":"2010","journal-title":"Virol. J."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"347","DOI":"10.4149\/av_2019_408","article-title":"Different mechanisms of the protection against influenza A infection mediated by broadly reactive HA2-specific antibodies","volume":"63","year":"2019","journal-title":"Acta Virol."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"247","DOI":"10.4149\/av_2013_02_247","article-title":"HA2 glycopolypeptide of influenza A virus and antiviral immunity","volume":"57","author":"Mucha","year":"2013","journal-title":"Acta Virol."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1006\/viro.1999.9716","article-title":"Role of Hemagglutinin Cleavage for the Pathogenicity of Influenza Virus","volume":"258","author":"Steinhauer","year":"1999","journal-title":"Virology"},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1002\/rmv.657","article-title":"Novel insights into proteolytic cleavage of influenza virus hemagglutinin","volume":"20","author":"Bertram","year":"2010","journal-title":"Rev. Med. Virol."},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"5605","DOI":"10.1128\/JVI.00140-10","article-title":"Cleavage of Influenza Virus Hemagglutinin by Airway Proteases TMPRSS2 and HAT Differs in Subcellular Localization and Susceptibility to Protease Inhibitors","volume":"84","author":"Freuer","year":"2010","journal-title":"J. Virol."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1146\/annurev.biochem.69.1.531","article-title":"Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin","volume":"69","author":"Skehel","year":"2000","journal-title":"Annu. Rev. Biochem."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1007\/s00705-002-0932-1","article-title":"Inhibition of fusion activity of influenza A haemagglutinin mediated by HA2-specific monoclonal antibodies","volume":"148","author":"Mucha","year":"2003","journal-title":"Arch. Virol."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"121","DOI":"10.4149\/av_2016_02_121","article-title":"The role of fusion activity of influenza A viruses in their biological properties","volume":"60","year":"2016","journal-title":"Acta Virol."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"1282","DOI":"10.1099\/jgv.0.001305","article-title":"Biological properties of influenza A virus mutants with amino acid substitutions in the HA2 glycoprotein of the HA1\/HA2 interaction region","volume":"100","author":"Fodor","year":"2019","journal-title":"J. Gen. Virol."},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1111\/2049-632X.12053","article-title":"Activation of influenza viruses by proteases from host cells and bacteria in the human airway epithelium","volume":"69","author":"Klenk","year":"2013","journal-title":"Pathog. Dis."},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1038\/325536a0","article-title":"Role of Staphylococcus protease in the development of influenza pneumonia","volume":"325","author":"Tashiro","year":"1987","journal-title":"Nature"},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1093\/infdis\/166.4.783","article-title":"Interactions between Bacteria and Influenza A Virus in the Development of Influenza Pneumonia","volume":"166","author":"Scheiblauer","year":"1992","journal-title":"J. Infect. Dis."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1099\/0022-1317-36-1-151","article-title":"Further Studies on the Activation of Influenza Virus by Proteolytic Cleavage of the Haemagglutinin","volume":"36","author":"Klenk","year":"1977","journal-title":"J. Gen. Virol."},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1590\/S0036-46652005000500007","article-title":"Co-infection between influenza virus and flagellated bacteria","volume":"47","author":"Mancini","year":"2005","journal-title":"Rev. Inst. Med. Trop. Sao Paulo"},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"7579","DOI":"10.1128\/jvi.71.10.7579-7585.1997","article-title":"Cleavage of influenza A virus H1 hemagglutinin by swine respiratory bacterial proteases","volume":"71","author":"Callan","year":"1997","journal-title":"J. Virol."},{"key":"ref_227","doi-asserted-by":"crossref","unstructured":"Berri, F., Rimmelzwaan, G.F., Hanss, M., Albina, E., Foucault-Grunenwald, M.-L., L\u00ea, V.B., Vogelzang-van Trierum, S.E., Gil, P., Camerer, E., and Martinez, D. (2013). Plasminogen Controls Inflammation and Pathogenesis of Influenza Virus Infections via Fibrinolysis. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003229"},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"5161","DOI":"10.1128\/JVI.00210-13","article-title":"Plasmin-Mediated Activation of Pandemic H1N1 Influenza Virus Hemagglutinin Is Independent of the Viral Neuraminidase","volume":"87","author":"Tse","year":"2013","journal-title":"J. Virol."},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.virol.2015.03.023","article-title":"Modification of the hemagglutinin cleavage site allows indirect activation of avian influenza virus H9N2 by bacterial staphylokinase","volume":"482","author":"Tse","year":"2015","journal-title":"Virology"},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1006\/mpat.1998.0262","article-title":"Surface bound plasmin promotes migration of Streptococcus pneumoniae through reconstituted basement membranes","volume":"26","author":"Eberhard","year":"1999","journal-title":"Microb. Pathog."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"85","DOI":"10.3389\/fcimb.2013.00085","article-title":"Interaction of streptococcal plasminogen binding proteins with the host fibrinolytic system","volume":"3","author":"Fulde","year":"2013","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1160\/TH13-05-0421","article-title":"Pneumococcal phosphoglycerate kinase interacts with plasminogen and its tissue activator","volume":"111","author":"Fulde","year":"2014","journal-title":"J. Thromb. Haemost."},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"609","DOI":"10.2217\/fmb.12.29","article-title":"Interactions between Streptococcus pneumoniae and influenza virus: A mutually beneficial relationship?","volume":"7","author":"Short","year":"2012","journal-title":"Future Microbiol."},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.ijmm.2010.06.008","article-title":"Viral hemagglutinin is involved in promoting the internalisation of Staphylococcus aureus into human pneumocytes during influenza A H1N1 virus infection","volume":"301","author":"Passariello","year":"2011","journal-title":"Int. J. Med. Microbiol."},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"4104","DOI":"10.1128\/JVI.77.7.4104-4112.2003","article-title":"Influenza A Virus-Infected Hosts Boost an Invasive Type of Streptococcus pyogenes Infection in Mice","volume":"77","author":"Okamoto","year":"2003","journal-title":"J. Virol."},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1093\/oxfordjournals.jmicro.a023870","article-title":"Binding of influenza type A viruses to group B Streptococcus and haemagglutination by virus-bound bacteria","volume":"49","author":"Hosaka","year":"2000","journal-title":"J. Electron. Microsc."},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1186\/1743-422X-10-128","article-title":"Influenza A virus induced bacterial otitis media is independent of virus tropism for \u03b12,6-linked sialic acid","volume":"10","author":"Short","year":"2013","journal-title":"Virol. J."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"39","DOI":"10.3389\/fmicb.2019.00039","article-title":"Influenza Virus Neuraminidase Structure and Functions","volume":"10","author":"McAuley","year":"2019","journal-title":"Front. Microbiol."},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1128\/jvi.67.2.759-764.1993","article-title":"Biologic importance of neuraminidase stalk length in influenza A virus","volume":"67","author":"Castrucci","year":"1993","journal-title":"J. Virol."},{"key":"ref_240","doi-asserted-by":"crossref","unstructured":"Kosik, I., and Yewdell, J.W. (2019). Influenza Hemagglutinin and Neuraminidase: Yin-Yang Proteins Coevolving to Thwart Immunity. Viruses, 11.","DOI":"10.3390\/v11040346"},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"5258","DOI":"10.1128\/JVI.78.10.5258-5269.2004","article-title":"Role of transmembrane domain and cytoplasmic tail amino acid sequences of influenza a virus neuraminidase in raft association and virus budding","volume":"78","author":"Barman","year":"2004","journal-title":"J. Virol."},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.1093\/emboj\/16.6.1236","article-title":"Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape","volume":"16","author":"Jin","year":"1997","journal-title":"EMBO J."},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1128\/jvi.70.2.873-879.1996","article-title":"The cytoplasmic tail of influenza A virus neuraminidase (NA) affects NA incorporation into virions, virion morphology, and virulence in mice but is not essential for virus replication","volume":"70","author":"Mitnaul","year":"1996","journal-title":"J. Virol."},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1016\/j.tim.2019.03.001","article-title":"Influenza Neuraminidase: Underrated Role in Receptor Binding","volume":"27","author":"Wen","year":"2019","journal-title":"Trends. Microbiol."},{"key":"ref_245","doi-asserted-by":"crossref","unstructured":"Du, R., Cui, Q., and Rong, L. (2019). Competitive Cooperation of Hemagglutinin and Neuraminidase during Influenza A Virus Entry. Viruses, 11.","DOI":"10.3390\/v11050458"},{"key":"ref_246","doi-asserted-by":"crossref","unstructured":"Su, B., Wurtzer, S., Rameix-Welti, M.A., Dwyer, D., van der Werf, S., Naffakh, N., Clavel, F., and Labrosse, B. (2009). Enhancement of the influenza A hemagglutinin (HA)-mediated cell-cell fusion and virus entry by the viral neuraminidase (NA). PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0008495"},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1021\/acs.bioconjchem.6b00050","article-title":"Pneumococcal Neuraminidase Substrates Identified through Comparative Proteomics Enabled by Chemoselective Labeling","volume":"27","author":"McCombs","year":"2016","journal-title":"Bioconjug. Chem."},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"3360","DOI":"10.1128\/IAI.01442-05","article-title":"Variation in the presence of neuraminidase genes among Streptococcus pneumoniae isolates with identical sequence types","volume":"74","author":"Pettigrew","year":"2006","journal-title":"Infect. Immun."},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1016\/j.jmb.2011.04.016","article-title":"Structural basis for Streptococcus pneumoniae NanA inhibition by influenza antivirals zanamivir and oseltamivir carboxylate","volume":"409","author":"Gut","year":"2011","journal-title":"J. Mol. Biol."},{"key":"ref_250","doi-asserted-by":"crossref","first-page":"357","DOI":"10.3389\/fmicb.2016.00357","article-title":"Dual Acting Neuraminidase Inhibitors Open New Opportunities to Disrupt the Lethal Synergism between Streptococcus pneumoniae and Influenza Virus","volume":"7","author":"Walther","year":"2016","journal-title":"Front. Microbiol."},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1016\/S0140-6736(99)11433-8","article-title":"Influenza virus neuraminidase inhibitors","volume":"355","author":"Gubareva","year":"2000","journal-title":"Lancet"},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1086\/430954","article-title":"influenza virus neuraminidase contributes to secondary bacterial pneumonia","volume":"192","author":"Peltola","year":"2005","journal-title":"J. Infect. Dis."},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"2466","DOI":"10.4049\/jimmunol.180.4.2466","article-title":"Role of galectin-3 in leukocyte recruitment in a murine model of lung infection by Streptococcus pneumoniae","volume":"180","author":"Nieminen","year":"2008","journal-title":"J. Immunol."},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1016\/j.sbi.2007.09.002","article-title":"Functions of cell surface galectin-glycoprotein lattices","volume":"17","author":"Rabinovich","year":"2007","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"1408","DOI":"10.1091\/mbc.e08-07-0786","article-title":"Galectin-1 induces reversible phosphatidylserine exposure at the plasma membrane","volume":"20","author":"Stowell","year":"2009","journal-title":"Mol. Biol. Cell."},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1038\/nrmicro2146","article-title":"Roles of galectins in infection","volume":"7","author":"Vasta","year":"2009","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_257","doi-asserted-by":"crossref","first-page":"e17","DOI":"10.1017\/S1462399408000719","article-title":"Galectins: Structure, function and therapeutic potential","volume":"10","author":"Yang","year":"2008","journal-title":"Expert Rev. Mol. Med."},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"111713","DOI":"10.1016\/j.biopha.2021.111713","article-title":"Regulatory roles of galectins on influenza A virus and their potential as a therapeutic strategy","volume":"139","author":"Yang","year":"2021","journal-title":"Biomed. Pharmacother."},{"key":"ref_259","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.3389\/fmicb.2020.01293","article-title":"Galectin-1 ameliorates influenza A H1N1pdm09 virus-induced acute lung injury","volume":"11","author":"Bao","year":"2020","journal-title":"Front. Microbiol."},{"key":"ref_260","first-page":"5","article-title":"Inhibition of influenza A virus infection by Galectin-9","volume":"61","author":"Hattori","year":"2013","journal-title":"Jpn. J. Vet. Res."},{"key":"ref_261","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1620\/tjem.232.263","article-title":"Increased levels of plasma galectin-9 in patients with influenza virus infection","volume":"232","author":"Katoh","year":"2014","journal-title":"Tohoku J. Exp. Med."},{"key":"ref_262","doi-asserted-by":"crossref","first-page":"19001","DOI":"10.1073\/pnas.1107087108","article-title":"T cell immunoglobulin and mucin protein-3 (Tim-3)\/galectin-9 interaction regulates influenza A virus-specific humoral and CD8 T-cell responses","volume":"108","author":"Sharma","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_263","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1016\/j.ajpath.2017.12.014","article-title":"Galectin-3 enhances avian H5N1 influenza A virus-induced pulmonary inflammation by promoting NLRP3 inflammasome activation","volume":"188","author":"Chen","year":"2018","journal-title":"Am. J. Pathol."},{"key":"ref_264","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.ejphar.2014.05.028","article-title":"Antiviral activity of aloe-emodin against influenza A virus via galectin-3 up-regulation","volume":"738","author":"Li","year":"2014","journal-title":"Eur. J. Pharmacol."},{"key":"ref_265","doi-asserted-by":"crossref","unstructured":"Lin, C.Y., Yang, Z.S., Wang, W.H., Urbina, A.N., Lin, Y.T., Huang, J.C., Liu, F.T., and Wang, S.F. (2021). The Antiviral Role of Galectins toward Influenza A Virus Infection\u2014An Alternative Strategy for Influenza Therapy. Pharmaceuticals, 14.","DOI":"10.3390\/ph14050490"},{"key":"ref_266","doi-asserted-by":"crossref","first-page":"2037","DOI":"10.1016\/j.bmc.2013.01.028","article-title":"Design and synthesis of glycoprotein-based multivalent glyco-ligands for influenza hemagglutinin and human galectin-3","volume":"21","author":"Wang","year":"2013","journal-title":"Bioorg. Med. Chem."},{"key":"ref_267","doi-asserted-by":"crossref","first-page":"925","DOI":"10.1016\/j.jmii.2019.09.005","article-title":"The role of galectins in virus infection\u2014A systemic literature review","volume":"53","author":"Wang","year":"2020","journal-title":"J. Microbiol. Immunol. Infect."},{"key":"ref_268","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1016\/j.femsre.2004.12.003","article-title":"Role of apoptosis and cytokines in influenza virus morbidity","volume":"29","author":"Brydon","year":"2005","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_269","doi-asserted-by":"crossref","first-page":"8624","DOI":"10.1128\/jvi.70.12.8624-8629.1996","article-title":"Influenza virus neuraminidase activates latent transforming growth factor beta","volume":"70","author":"Hinshaw","year":"1996","journal-title":"J. Virol."},{"key":"ref_270","doi-asserted-by":"crossref","unstructured":"Carlson, C.M., Turpin, E.A., Moser, L.A., O\u2019Brien, K.B., Cline, T.D., Jones, J.C., Tumpey, T.M., Katz, J.M., Kelley, L.A., and Gauldie, J. (2010). Transforming growth factor-\u03b2: Activation by neuraminidase and role in highly pathogenic H5N1 influenza pathogenesis. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1001136"},{"key":"ref_271","doi-asserted-by":"crossref","unstructured":"Chen, Q., Huang, S., Chen, J., Zhang, S., and Chen, Z. (2013). NA proteins of influenza A viruses H1N1\/2009, H5N1, and H9N2 show differential effects on infection initiation, virus release, and cell-cell fusion. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0054334"},{"key":"ref_272","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1146\/annurev.immunol.16.1.137","article-title":"Regulation of immune responses by TGF-beta","volume":"16","author":"Letterio","year":"1998","journal-title":"Annu. Rev. Immunol."},{"key":"ref_273","doi-asserted-by":"crossref","first-page":"e01335-19","DOI":"10.1128\/mBio.01335-19","article-title":"Allergic Airway Disease Prevents Lethal Synergy of Influenza A Virus-Streptococcus pneumoniae Coinfection","volume":"10","author":"Roberts","year":"2019","journal-title":"MBio"},{"key":"ref_274","doi-asserted-by":"crossref","first-page":"743","DOI":"10.3389\/fimmu.2018.00743","article-title":"Influenza Virus: A Master Tactician in Innate Immune Evasion and Novel Therapeutic Interventions","volume":"9","author":"Hsu","year":"2018","journal-title":"Front. Immunol."},{"key":"ref_275","doi-asserted-by":"crossref","unstructured":"Jia, D., Rahbar, R., Chan, R.W., Lee, S.M., Chan, M.C., Wang, B.X., Baker, D.P., Sun, B., Peiris, J.S., and Nicholls, J.M. (2010). Influenza virus non-structural protein 1 (NS1) disrupts interferon signaling. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0013927"},{"key":"ref_276","doi-asserted-by":"crossref","unstructured":"Kim, H.J., Jeong, M.S., and Jang, S.B. (2021). Structure and Activities of the NS1 Influenza Protein and Progress in the Development of Small-Molecule Drugs. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22084242"},{"key":"ref_277","first-page":"73","article-title":"The NS1 protein: A multitasking virulence factor","volume":"386","author":"Ayllon","year":"2015","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"ref_278","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.coviro.2015.01.007","article-title":"Functions of the influenza A virus NS1 protein in antiviral defense","volume":"12","author":"Krug","year":"2015","journal-title":"Curr. Opin. Virol."},{"key":"ref_279","doi-asserted-by":"crossref","first-page":"336","DOI":"10.2174\/187152607783018754","article-title":"The influenza virus NS1 protein: Inhibitor of innate and adaptive immunity","volume":"7","year":"2007","journal-title":"Infect. Disord. Drug Targets"},{"key":"ref_280","doi-asserted-by":"crossref","first-page":"6295","DOI":"10.1128\/JVI.02381-05","article-title":"Influenza virus evades innate and adaptive immunity via the NS1 protein","volume":"80","author":"Marukian","year":"2006","journal-title":"J. Virol."},{"key":"ref_281","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1006\/viro.1998.9508","article-title":"Influenza A virus lacking the NS1 gene replicates in interferon-deficient systems","volume":"252","author":"Egorov","year":"1998","journal-title":"Virology"},{"key":"ref_282","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1089\/vim.2018.0118","article-title":"A Novel Role for PDZ-Binding Motif of Influenza A Virus Nonstructural Protein 1 in Regulation of Host Susceptibility to Postinfluenza Bacterial Superinfections","volume":"32","author":"Shepardson","year":"2019","journal-title":"Viral Immunol."},{"key":"ref_283","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1146\/annurev-cellbio-100617-062903","article-title":"Cytoplasmic Mechanisms of Recognition and Defense of Microbial Nucleic Acids","volume":"34","author":"Hu","year":"2018","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_284","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1002\/jmv.24944","article-title":"MCPIP1 attenuates the innate immune response to influenza A virus by suppressing RIG-I expression in lung epithelial cells","volume":"90","author":"Sun","year":"2018","journal-title":"J. Med. Virol."},{"key":"ref_285","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1165\/rcmb.2006-0283RC","article-title":"NS1 protein of influenza A virus inhibits the function of intracytoplasmic pathogen sensor, RIG-I","volume":"36","author":"Guo","year":"2007","journal-title":"Am. J. Respir. Cell Mol."},{"key":"ref_286","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1128\/JVI.01265-06","article-title":"Inhibition of retinoic acid-inducible gene I-mediated induction of beta interferon by the NS1 protein of influenza A virus","volume":"81","author":"Mibayashi","year":"2007","journal-title":"J. Virol."},{"key":"ref_287","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1126\/science.1132998","article-title":"RIG-I-mediated antiviral responses to single-stranded RNA bearing 5\u2032-phosphates","volume":"314","author":"Pichlmair","year":"2006","journal-title":"Science"},{"key":"ref_288","doi-asserted-by":"crossref","first-page":"8389","DOI":"10.1128\/JVI.00041-16","article-title":"To conquer the host, influenza virus is packing it in: Interferon-antagonistic strategies beyond NS1","volume":"90","author":"Weber","year":"2016","journal-title":"J. Virol."},{"key":"ref_289","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1515\/BC.2008.148","article-title":"Influenza viruses and the NF-kappaB signaling pathway\u2014towards a novel concept of antiviral therapy","volume":"389","author":"Ludwig","year":"2008","journal-title":"Biol. Chem."},{"key":"ref_290","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1038\/41493","article-title":"A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB","volume":"388","author":"DiDonato","year":"1997","journal-title":"Nature"},{"key":"ref_291","doi-asserted-by":"crossref","first-page":"1278","DOI":"10.1128\/MCB.20.4.1278-1290.2000","article-title":"NF-kappaB activation by double-stranded-RNA-activated protein kinase (PKR) is mediated through NF-kappaB-inducing kinase and IkappaB kinase","volume":"20","author":"Mogensen","year":"2000","journal-title":"Mol. Cell. Biol."},{"key":"ref_292","doi-asserted-by":"crossref","first-page":"11566","DOI":"10.1128\/JVI.74.24.11566-11573.2000","article-title":"Influenza A virus NS1 protein prevents activation of NF-kappaB and induction of alpha\/beta interferon","volume":"74","author":"Wang","year":"2000","journal-title":"J. Virol."},{"key":"ref_293","doi-asserted-by":"crossref","first-page":"3764","DOI":"10.1128\/IAI.00298-15","article-title":"Influenza and Bacterial Superinfection: Illuminating the Immunologic Mechanisms of Disease","volume":"83","author":"Robinson","year":"2015","journal-title":"Infect Immun."}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/14\/5\/1064\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T23:11:30Z","timestamp":1760137890000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/14\/5\/1064"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,5,16]]},"references-count":293,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2022,5]]}},"alternative-id":["v14051064"],"URL":"https:\/\/doi.org\/10.3390\/v14051064","relation":{},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,5,16]]}}}