Protective human monoclonal antibodies target conserved sites of vulnerability on the underside of influenza virus neuraminidase
Continuously evolving influenza viruses cause seasonal epidemics and pose global pandemic threats. Although viral neuraminidase (NA) is an effective drug and vaccine target, our understanding of the NA antigenic landscape still remains incomplete. Here, we describe NA-specific human antibodies that...
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| Published in | Immunity (Cambridge, Mass.) Vol. 57; no. 3; pp. 574 - 586.e7 |
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| Main Authors | , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
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United States
Elsevier Inc
12.03.2024
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| Abstract | Continuously evolving influenza viruses cause seasonal epidemics and pose global pandemic threats. Although viral neuraminidase (NA) is an effective drug and vaccine target, our understanding of the NA antigenic landscape still remains incomplete. Here, we describe NA-specific human antibodies that target the underside of the NA globular head domain, inhibit viral propagation of a wide range of human H3N2, swine-origin variant H3N2, and H2N2 viruses, and confer both pre- and post-exposure protection against lethal H3N2 infection in mice. Cryo-EM structures of two such antibodies in complex with NA reveal non-overlapping epitopes covering the underside of the NA head. These sites are highly conserved among N2 NAs yet inaccessible unless the NA head tilts or dissociates. Our findings help guide the development of effective countermeasures against ever-changing influenza viruses by identifying hidden conserved sites of vulnerability on the NA underside.
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•Isolation of broadly cross-reactive and protective N2 NA-targeting human antibodies•Cryo-EM structures of two broadly cross-reactive antibodies in complex with N2 NA•Identification of conserved non-overlapping epitopes on the underside of NA head•Detection of antibodies to the NA underside epitopes in human convalescent samples
Influenza neuraminidase (NA) is underappreciated as a vaccine target owing to its incomplete epitope landscape. Lederhofer et al. isolated human monoclonal antibodies to NA underside (i.e., dark side) epitopes with broad cross-reactivity across N2 subtype and protective efficacy in pre- and post-exposure settings, providing insights for NA-based vaccine design. |
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| AbstractList | Continuously evolving influenza viruses cause seasonal epidemics and pose global pandemic threats. Although viral neuraminidase (NA) is an effective drug and vaccine target, our understanding of the NA antigenic landscape still remains incomplete. Here, we describe NA-specific human antibodies that target the underside of the NA globular head domain, inhibit viral propagation of a wide range of human H3N2, swine-origin variant H3N2, and H2N2 viruses, and confer both pre- and post-exposure protection against lethal H3N2 infection in mice. Cryo-EM structures of two such antibodies in complex with NA reveal non-overlapping epitopes covering the underside of the NA head. These sites are highly conserved among N2 NAs yet inaccessible unless the NA head tilts or dissociates. Our findings help guide the development of effective countermeasures against ever-changing influenza viruses by identifying hidden conserved sites of vulnerability on the NA underside.
[Display omitted]
•Isolation of broadly cross-reactive and protective N2 NA-targeting human antibodies•Cryo-EM structures of two broadly cross-reactive antibodies in complex with N2 NA•Identification of conserved non-overlapping epitopes on the underside of NA head•Detection of antibodies to the NA underside epitopes in human convalescent samples
Influenza neuraminidase (NA) is underappreciated as a vaccine target owing to its incomplete epitope landscape. Lederhofer et al. isolated human monoclonal antibodies to NA underside (i.e., dark side) epitopes with broad cross-reactivity across N2 subtype and protective efficacy in pre- and post-exposure settings, providing insights for NA-based vaccine design. Continuously evolving influenza viruses cause seasonal epidemics and pose global pandemic threats. Although viral neuraminidase (NA) is an effective drug and vaccine target, our understanding of the NA antigenic landscape still remains incomplete. Here, we describe NA-specific human antibodies that target the underside of the NA globular head domain, inhibit viral propagation of a wide range of human H3N2, swine-origin variant H3N2, and H2N2 viruses, and confer both pre- and post-exposure protection against lethal H3N2 infection in mice. Cryo-EM structures of two such antibodies in complex with NA reveal non-overlapping epitopes covering the underside of the NA head. These sites are highly conserved among N2 NAs yet inaccessible unless the NA head tilts or dissociates. Our findings help guide the development of effective countermeasures against ever-changing influenza viruses by identifying hidden conserved sites of vulnerability on the NA underside. Continuously evolving influenza viruses cause seasonal epidemics and pose global pandemic threats. Although viral neuraminidase (NA) is an effective drug and vaccine target, our understanding of the NA antigenic landscape still remains incomplete. Here, we describe NA-specific human antibodies that target the underside of the NA globular head domain, inhibit viral propagation of a wide range of human H3N2, swine-origin variant H3N2, and H2N2 viruses, and confer both pre- and post-exposure protection against lethal H3N2 infection in mice. Cryo-EM structures of two such antibodies in complex with NA reveal non-overlapping epitopes covering the underside of the NA head. These sites are highly conserved among N2 NAs yet inaccessible unless the NA head tilts or dissociates. Our findings help guide the development of effective countermeasures against ever-changing influenza viruses by identifying hidden conserved sites of vulnerability on the NA underside. Influenza neuraminidase (NA) is underappreciated as a vaccine target due to its incomplete epitope landscape. Lederhofer et al. isolated human monoclonal antibodies to NA underside (i.e., dark side) epitopes with broad cross-reactivity across N2 subtype and protective efficacy in pre- and post-exposure settings, providing insights for NA-based vaccine design. Continuously evolving influenza viruses cause seasonal epidemics and pose global pandemic threats. Although viral neuraminidase (NA) is an effective drug and vaccine target, our understanding of the NA antigenic landscape still remains incomplete. Here, we describe NA-specific human antibodies that target the underside of the NA globular head domain, inhibit viral propagation of a wide range of human H3N2, swine-origin variant H3N2, and H2N2 viruses, and confer both pre- and post-exposure protection against lethal H3N2 infection in mice. Cryo-EM structures of two such antibodies in complex with NA reveal non-overlapping epitopes covering the underside of the NA head. These sites are highly conserved among N2 NAs yet inaccessible unless the NA head tilts or dissociates. Our findings help guide the development of effective countermeasures against ever-changing influenza viruses by identifying hidden conserved sites of vulnerability on the NA underside.Continuously evolving influenza viruses cause seasonal epidemics and pose global pandemic threats. Although viral neuraminidase (NA) is an effective drug and vaccine target, our understanding of the NA antigenic landscape still remains incomplete. Here, we describe NA-specific human antibodies that target the underside of the NA globular head domain, inhibit viral propagation of a wide range of human H3N2, swine-origin variant H3N2, and H2N2 viruses, and confer both pre- and post-exposure protection against lethal H3N2 infection in mice. Cryo-EM structures of two such antibodies in complex with NA reveal non-overlapping epitopes covering the underside of the NA head. These sites are highly conserved among N2 NAs yet inaccessible unless the NA head tilts or dissociates. Our findings help guide the development of effective countermeasures against ever-changing influenza viruses by identifying hidden conserved sites of vulnerability on the NA underside. |
| Author | Kanekiyo, Masaru Skertic, Michelle Syeda, Hubza Z. Nguyen, Lam Rawi, Reda Tsybovsky, Yaroslav Schaub, Andrew J. King, Neil P. Lederhofer, Julia Kwong, Peter D. Stephens, Tyler Andrews, Sarah F. Yap, Christina Creanga, Adrian Graham, Barney S. Raab, Julie E. McDermott, Adrian B. Gillespie, Rebecca A. Fisher, Brian E. |
| AuthorAffiliation | 4 Institute for Protein Design, University of Washington, Seattle, WA 98195, United States 1 Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, United States 2 Vaccine Research Center Electron Microscopy Unit, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research sponsored by the National Cancer Institute, Frederick, MD 21702, United States 6 Present address: Sanofi, Lyon, 69007, France 5 Present address: Morehouse School of Medicine, Atlanta, GA 30310, United States 3 Department of Biochemistry, University of Washington, Seattle, WA 98195, United States 7 Lead contact |
| AuthorAffiliation_xml | – name: 3 Department of Biochemistry, University of Washington, Seattle, WA 98195, United States – name: 7 Lead contact – name: 2 Vaccine Research Center Electron Microscopy Unit, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research sponsored by the National Cancer Institute, Frederick, MD 21702, United States – name: 5 Present address: Morehouse School of Medicine, Atlanta, GA 30310, United States – name: 1 Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, United States – name: 4 Institute for Protein Design, University of Washington, Seattle, WA 98195, United States – name: 6 Present address: Sanofi, Lyon, 69007, France |
| Author_xml | – sequence: 1 givenname: Julia surname: Lederhofer fullname: Lederhofer, Julia organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 2 givenname: Yaroslav surname: Tsybovsky fullname: Tsybovsky, Yaroslav organization: Vaccine Research Center Electron Microscopy Unit, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research sponsored by the National Cancer Institute, Frederick, MD 21702, USA – sequence: 3 givenname: Lam surname: Nguyen fullname: Nguyen, Lam organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 4 givenname: Julie E. surname: Raab fullname: Raab, Julie E. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 5 givenname: Adrian surname: Creanga fullname: Creanga, Adrian organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 6 givenname: Tyler surname: Stephens fullname: Stephens, Tyler organization: Vaccine Research Center Electron Microscopy Unit, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research sponsored by the National Cancer Institute, Frederick, MD 21702, USA – sequence: 7 givenname: Rebecca A. surname: Gillespie fullname: Gillespie, Rebecca A. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 8 givenname: Hubza Z. surname: Syeda fullname: Syeda, Hubza Z. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 9 givenname: Brian E. surname: Fisher fullname: Fisher, Brian E. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 10 givenname: Michelle surname: Skertic fullname: Skertic, Michelle organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 11 givenname: Christina surname: Yap fullname: Yap, Christina organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 12 givenname: Andrew J. surname: Schaub fullname: Schaub, Andrew J. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 13 givenname: Reda surname: Rawi fullname: Rawi, Reda organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 14 givenname: Peter D. surname: Kwong fullname: Kwong, Peter D. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 15 givenname: Barney S. surname: Graham fullname: Graham, Barney S. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 16 givenname: Adrian B. surname: McDermott fullname: McDermott, Adrian B. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 17 givenname: Sarah F. surname: Andrews fullname: Andrews, Sarah F. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 18 givenname: Neil P. surname: King fullname: King, Neil P. organization: Department of Biochemistry, University of Washington, Seattle, WA 98195, USA – sequence: 19 givenname: Masaru orcidid: 0000-0001-5767-1532 surname: Kanekiyo fullname: Kanekiyo, Masaru email: kanekiyom@nih.gov organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/38430907$$D View this record in MEDLINE/PubMed |
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| Copyright | 2024 Published by Elsevier Inc. |
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| Keywords | influenza B cell dark side NA bnab underside neuraminidase antigenic site epitope cryo-EM human monoclonal antibody mAb |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Conceptualization, J.L. and M.K.; formal analysis, J.L., Y.T., S.F.A. and M.K.; investigation, J.L., Y.T., L.N., J.E.R., A.C., T.S., R.A.G., H.Z.S., B.E.F., M.S., C.Y., A.S., R.R., S.F.A., N.P.K. and M.K.; resources, A.C. and M.S.; writing – original draft, J.L., Y.T., N.P.K. and M.K.; writing – review and editing, all authors; supervision, P.D.K., B.S.G., A.B.M., S.F.A., N.P.K. and M.K.; funding acquisition, P.D.K., B.S.G., A.B.M. and M.K. Author contributions |
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| Title | Protective human monoclonal antibodies target conserved sites of vulnerability on the underside of influenza virus neuraminidase |
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