Mapping the interaction sites of human and avian influenza A viruses and complement factor H
The complement system is an innate immune mechanism against microbial infections. It involves a cascade of effector molecules that is activated via classical, lectin and alternative pathways. Consequently, many pathogens bind to or incorporate in their structures host negative regulators of the comp...
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Published in | Frontiers in immunology Vol. 15; p. 1352022 |
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Main Authors | , , , , , , , , , , |
Format | Journal Article |
Language | English |
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18.04.2024
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Abstract | The complement system is an innate immune mechanism against microbial infections. It involves a cascade of effector molecules that is activated via classical, lectin and alternative pathways. Consequently, many pathogens bind to or incorporate in their structures host negative regulators of the complement pathways as an evasion mechanism. Factor H (FH) is a negative regulator of the complement alternative pathway that protects "self" cells of the host from non-specific complement attack. FH has been shown to bind viruses including human influenza A viruses (IAVs). In addition to its involvement in the regulation of complement activation, FH has also been shown to perform a range of functions on its own including its direct interaction with pathogens. Here, we show that human FH can bind directly to IAVs of both human and avian origin, and the interaction is mediated via the IAV surface glycoprotein haemagglutinin (HA). HA bound to common pathogen binding footprints on the FH structure, complement control protein modules, CCP 5-7 and CCP 15-20. The FH binding to H1 and H3 showed that the interaction overlapped with the receptor binding site of both HAs, but the footprint was more extensive for the H3 HA than the H1 HA. The HA - FH interaction impeded the initial entry of H1N1 and H3N2 IAV strains but its impact on viral multicycle replication in human lung cells was strain-specific. The H3N2 virus binding to cells was significantly inhibited by preincubation with FH, whereas there was no alteration in replicative rate and progeny virus release for human H1N1, or avian H9N2 and H5N3 IAV strains. We have mapped the interaction between FH and IAV, the
significance of which for the virus or host is yet to be elucidated. |
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AbstractList | The complement system is an innate immune mechanism against microbial infections. It involves a cascade of effector molecules that is activated via classical, lectin and alternative pathways. Consequently, many pathogens bind to or incorporate in their structures host negative regulators of the complement pathways as an evasion mechanism. Factor H (FH) is a negative regulator of the complement alternative pathway that protects “self” cells of the host from non-specific complement attack. FH has been shown to bind viruses including human influenza A viruses (IAVs). In addition to its involvement in the regulation of complement activation, FH has also been shown to perform a range of functions on its own including its direct interaction with pathogens. Here, we show that human FH can bind directly to IAVs of both human and avian origin, and the interaction is mediated via the IAV surface glycoprotein haemagglutinin (HA). HA bound to common pathogen binding footprints on the FH structure, complement control protein modules, CCP 5-7 and CCP 15-20. The FH binding to H1 and H3 showed that the interaction overlapped with the receptor binding site of both HAs, but the footprint was more extensive for the H3 HA than the H1 HA. The HA - FH interaction impeded the initial entry of H1N1 and H3N2 IAV strains but its impact on viral multicycle replication in human lung cells was strain-specific. The H3N2 virus binding to cells was significantly inhibited by preincubation with FH, whereas there was no alteration in replicative rate and progeny virus release for human H1N1, or avian H9N2 and H5N3 IAV strains. We have mapped the interaction between FH and IAV, the
in vivo
significance of which for the virus or host is yet to be elucidated. The complement system is an innate immune mechanism against microbial infections. It involves a cascade of effector molecules that is activated via classical, lectin and alternative pathways. Consequently, many pathogens bind to or incorporate in their structures host negative regulators of the complement pathways as an evasion mechanism. Factor H (FH) is a negative regulator of the complement alternative pathway that protects "self" cells of the host from non-specific complement attack. FH has been shown to bind viruses including human influenza A viruses (IAVs). In addition to its involvement in the regulation of complement activation, FH has also been shown to perform a range of functions on its own including its direct interaction with pathogens. Here, we show that human FH can bind directly to IAVs of both human and avian origin, and the interaction is mediated via the IAV surface glycoprotein haemagglutinin (HA). HA bound to common pathogen binding footprints on the FH structure, complement control protein modules, CCP 5-7 and CCP 15-20. The FH binding to H1 and H3 showed that the interaction overlapped with the receptor binding site of both HAs, but the footprint was more extensive for the H3 HA than the H1 HA. The HA - FH interaction impeded the initial entry of H1N1 and H3N2 IAV strains but its impact on viral multicycle replication in human lung cells was strain-specific. The H3N2 virus binding to cells was significantly inhibited by preincubation with FH, whereas there was no alteration in replicative rate and progeny virus release for human H1N1, or avian H9N2 and H5N3 IAV strains. We have mapped the interaction between FH and IAV, the significance of which for the virus or host is yet to be elucidated. The complement system is an innate immune mechanism against microbial infections. It involves a cascade of effector molecules that is activated via classical, lectin and alternative pathways. Consequently, many pathogens bind to or incorporate in their structures host negative regulators of the complement pathways as an evasion mechanism. Factor H (FH) is a negative regulator of the complement alternative pathway that protects "self" cells of the host from non-specific complement attack. FH has been shown to bind viruses including human influenza A viruses (IAVs). In addition to its involvement in the regulation of complement activation, FH has also been shown to perform a range of functions on its own including its direct interaction with pathogens. Here, we show that human FH can bind directly to IAVs of both human and avian origin, and the interaction is mediated via the IAV surface glycoprotein haemagglutinin (HA). HA bound to common pathogen binding footprints on the FH structure, complement control protein modules, CCP 5-7 and CCP 15-20. The FH binding to H1 and H3 showed that the interaction overlapped with the receptor binding site of both HAs, but the footprint was more extensive for the H3 HA than the H1 HA. The HA - FH interaction impeded the initial entry of H1N1 and H3N2 IAV strains but its impact on viral multicycle replication in human lung cells was strain-specific. The H3N2 virus binding to cells was significantly inhibited by preincubation with FH, whereas there was no alteration in replicative rate and progeny virus release for human H1N1, or avian H9N2 and H5N3 IAV strains. We have mapped the interaction between FH and IAV, the in vivo significance of which for the virus or host is yet to be elucidated. |
Author | Iqbal, Munir Zipfel, Peter F Pathan, Ansar A Sadeyen, Jean-Remy Kishore, Uday Temperton, Nigel J Skerka, Christine Billington, Elizabeth Shelton, Holly Nal, Béatrice Rabeeah, Iman |
AuthorAffiliation | 7 Department of Veterinary Medicine, United Arab Emirates University , Al Ain , United Arab Emirates 1 Pirbright Institute , Woking , United Kingdom 5 Department of Infection Biology, Leibniz Institute for Natural Product Research and Infection Biology , Jena , Germany 6 Institute of Microbiology, Friedrich Schiller University , Jena , Germany 8 Zayed Centre for Biomedical Sciences, U.A.E. University , Al Ain , United Arab Emirates 4 Viral Pseudotype Unit, University of Kent , Chatham , United Kingdom 3 Aix-Marseille Université, CNRS, INSERM, CIML , Marseille , France 2 Biosciences, College of Health, Medicine and Life Sciences, Brunel University London , Uxbridge , United Kingdom |
AuthorAffiliation_xml | – name: 1 Pirbright Institute , Woking , United Kingdom – name: 6 Institute of Microbiology, Friedrich Schiller University , Jena , Germany – name: 2 Biosciences, College of Health, Medicine and Life Sciences, Brunel University London , Uxbridge , United Kingdom – name: 7 Department of Veterinary Medicine, United Arab Emirates University , Al Ain , United Arab Emirates – name: 8 Zayed Centre for Biomedical Sciences, U.A.E. University , Al Ain , United Arab Emirates – name: 4 Viral Pseudotype Unit, University of Kent , Chatham , United Kingdom – name: 3 Aix-Marseille Université, CNRS, INSERM, CIML , Marseille , France – name: 5 Department of Infection Biology, Leibniz Institute for Natural Product Research and Infection Biology , Jena , Germany |
Author_xml | – sequence: 1 givenname: Iman surname: Rabeeah fullname: Rabeeah, Iman organization: Biosciences, College of Health, Medicine and Life Sciences, Brunel University London, Uxbridge, United Kingdom – sequence: 2 givenname: Elizabeth surname: Billington fullname: Billington, Elizabeth organization: Pirbright Institute, Woking, United Kingdom – sequence: 3 givenname: Béatrice surname: Nal fullname: Nal, Béatrice organization: Aix-Marseille Université, CNRS, INSERM, CIML, Marseille, France – sequence: 4 givenname: Jean-Remy surname: Sadeyen fullname: Sadeyen, Jean-Remy organization: Pirbright Institute, Woking, United Kingdom – sequence: 5 givenname: Ansar A surname: Pathan fullname: Pathan, Ansar A organization: Biosciences, College of Health, Medicine and Life Sciences, Brunel University London, Uxbridge, United Kingdom – sequence: 6 givenname: Munir surname: Iqbal fullname: Iqbal, Munir organization: Pirbright Institute, Woking, United Kingdom – sequence: 7 givenname: Nigel J surname: Temperton fullname: Temperton, Nigel J organization: Viral Pseudotype Unit, University of Kent, Chatham, United Kingdom – sequence: 8 givenname: Peter F surname: Zipfel fullname: Zipfel, Peter F organization: Institute of Microbiology, Friedrich Schiller University, Jena, Germany – sequence: 9 givenname: Christine surname: Skerka fullname: Skerka, Christine organization: Department of Infection Biology, Leibniz Institute for Natural Product Research and Infection Biology, Jena, Germany – sequence: 10 givenname: Uday surname: Kishore fullname: Kishore, Uday organization: Zayed Centre for Biomedical Sciences, U.A.E. University, Al Ain, United Arab Emirates – sequence: 11 givenname: Holly surname: Shelton fullname: Shelton, Holly organization: Pirbright Institute, Woking, United Kingdom |
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Copyright | Copyright © 2024 Rabeeah, Billington, Nal, Sadeyen, Pathan, Iqbal, Temperton, Zipfel, Skerka, Kishore and Shelton. Copyright © 2024 Rabeeah, Billington, Nal, Sadeyen, Pathan, Iqbal, Temperton, Zipfel, Skerka, Kishore and Shelton 2024 Rabeeah, Billington, Nal, Sadeyen, Pathan, Iqbal, Temperton, Zipfel, Skerka, Kishore and Shelton |
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Keywords | entry inhibitor human influenza avian influenza complement factor H pseudotype influenza A virus |
Language | English |
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Title | Mapping the interaction sites of human and avian influenza A viruses and complement factor H |
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