A structural basis for antibody-mediated neutralization of Nipah virus reveals a site of vulnerability at the fusion glycoprotein apex.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
10 12 2019
Historique:
pubmed: 27 11 2019
medline: 9 4 2020
entrez: 27 11 2019
Statut: ppublish

Résumé

Nipah virus (NiV) is a highly pathogenic paramyxovirus that causes frequent outbreaks of severe neurologic and respiratory disease in humans with high case fatality rates. The 2 glycoproteins displayed on the surface of the virus, NiV-G and NiV-F, mediate host-cell attachment and membrane fusion, respectively, and are targets of the host antibody response. Here, we provide a molecular basis for neutralization of NiV through antibody-mediated targeting of NiV-F. Structural characterization of a neutralizing antibody (nAb) in complex with trimeric prefusion NiV-F reveals an epitope at the membrane-distal domain III (DIII) of the molecule, a region that undergoes substantial refolding during host-cell entry. The epitope of this monoclonal antibody (mAb66) is primarily protein-specific and we observe that glycosylation at the periphery of the interface likely does not inhibit mAb66 binding to NiV-F. Further characterization reveals that a Hendra virus-F-specific nAb (mAb36) and many antibodies in an antihenipavirus-F polyclonal antibody mixture (pAb835) also target this region of the molecule. Integrated with previously reported paramyxovirus F-nAb structures, these data support a model whereby the membrane-distal region of the F protein is targeted by the antibody-mediated immune response across henipaviruses. Notably, our domain-specific sequence analysis reveals no evidence of selective pressure at this region of the molecule, suggestive that functional constraints prevent immune-driven sequence variation. Combined, our data reveal the membrane-distal region of NiV-F as a site of vulnerability on the NiV surface.

Identifiants

pubmed: 31767754
pii: 1912503116
doi: 10.1073/pnas.1912503116
pmc: PMC6911215
doi:

Substances chimiques

Antibodies, Monoclonal 0
Antibodies, Neutralizing 0
Viral Fusion Proteins 0

Banques de données

PDB
['6T3F']

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

25057-25067

Subventions

Organisme : NIAID NIH HHS
ID : R01 AI123449
Pays : United States
Organisme : Medical Research Council
ID : MR/S007555/1
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 203141/Z/16/Z
Pays : United Kingdom
Organisme : Medical Research Council
ID : MR/N00065X/1
Pays : United Kingdom
Organisme : NIGMS NIH HHS
ID : R01 GM093939
Pays : United States
Organisme : Medical Research Council
ID : MR/N002091/1
Pays : United Kingdom
Organisme : NIAID NIH HHS
ID : R01 AI125536
Pays : United States
Organisme : NIAID NIH HHS
ID : F31 AI154739
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM008169
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI134384
Pays : United States
Organisme : Medical Research Council
ID : MR/L009528/1
Pays : United Kingdom
Organisme : Wellcome Trust
Pays : United Kingdom

Informations de copyright

Copyright © 2019 the Author(s). Published by PNAS.

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

Victoria A Avanzato (VA)

Division of Structural Biology, Wellcome Center for Human Genetics, University of Oxford, OX3 7BN Oxford, United Kingdom.
Laboratory of Virology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840.

Kasopefoluwa Y Oguntuyo (KY)

Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY 10029.

Marina Escalera-Zamudio (M)

Department of Zoology, Oxford University, OX1 3PS Oxford, United Kingdom.

Bernardo Gutierrez (B)

Department of Zoology, Oxford University, OX1 3PS Oxford, United Kingdom.

Michael Golden (M)

Department of Zoology, Oxford University, OX1 3PS Oxford, United Kingdom.

Sergei L Kosakovsky Pond (SL)

Institute for Genomics and Evolutionary Medicine, Temple University, Philadelphia, PA 19122.

Rhys Pryce (R)

Division of Structural Biology, Wellcome Center for Human Genetics, University of Oxford, OX3 7BN Oxford, United Kingdom.

Thomas S Walter (TS)

Division of Structural Biology, Wellcome Center for Human Genetics, University of Oxford, OX3 7BN Oxford, United Kingdom.

Jeffrey Seow (J)

Department of Infectious Diseases, King's College London, Guy's Hospital, SE1 9RT London, United Kingdom.

Katie J Doores (KJ)

Department of Infectious Diseases, King's College London, Guy's Hospital, SE1 9RT London, United Kingdom.

Oliver G Pybus (OG)

Department of Zoology, Oxford University, OX1 3PS Oxford, United Kingdom.

Vincent J Munster (VJ)

Laboratory of Virology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840.

Benhur Lee (B)

Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY 10029; Benhur.Lee@mssm.edu thomas.bowden@strubi.ox.ac.uk.
Global Virus Network (GVN) Center of Excellence, Center for Virology, Icahn School of Medicine at Mount Sinai, New York, NY 10029.

Thomas A Bowden (TA)

Division of Structural Biology, Wellcome Center for Human Genetics, University of Oxford, OX3 7BN Oxford, United Kingdom; Benhur.Lee@mssm.edu thomas.bowden@strubi.ox.ac.uk.

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