Structure of the Human Metapneumovirus Fusion Protein with Neutralizing Antibody Identifies a Pneumovirus Antigenic Site

Human metapneumovirus (HMPV) and respiratory syncytial virus (RSV) cause lower respiratory infections. The virus fusion (F) glycoprotein promotes membrane fusion by refolding from a metastable pre-fusion to a stable post-fusion conformation. F is also a major target of the neutralizing antibody resp...

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Autores principales: Wen, Xiaolin, Krause, Jens C., Leser, George P., Cox, Reagan G., Lamb, Robert A., Williams, John, Crowe, James E., Jardetzky, Theodore S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3546531/
https://www.ncbi.nlm.nih.gov/pubmed/22388735
http://dx.doi.org/10.1038/nsmb.2250
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author Wen, Xiaolin
Krause, Jens C.
Leser, George P.
Cox, Reagan G.
Lamb, Robert A.
Williams, John
Crowe, James E.
Jardetzky, Theodore S.
author_facet Wen, Xiaolin
Krause, Jens C.
Leser, George P.
Cox, Reagan G.
Lamb, Robert A.
Williams, John
Crowe, James E.
Jardetzky, Theodore S.
author_sort Wen, Xiaolin
collection PubMed
description Human metapneumovirus (HMPV) and respiratory syncytial virus (RSV) cause lower respiratory infections. The virus fusion (F) glycoprotein promotes membrane fusion by refolding from a metastable pre-fusion to a stable post-fusion conformation. F is also a major target of the neutralizing antibody response. Here we show that a potently neutralizing anti-HMPV antibody (DS7) binds a structurally invariant domain of F, identifying a new epitope that could be targeted in vaccine development.
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spelling pubmed-35465312013-01-16 Structure of the Human Metapneumovirus Fusion Protein with Neutralizing Antibody Identifies a Pneumovirus Antigenic Site Wen, Xiaolin Krause, Jens C. Leser, George P. Cox, Reagan G. Lamb, Robert A. Williams, John Crowe, James E. Jardetzky, Theodore S. Nat Struct Mol Biol Article Human metapneumovirus (HMPV) and respiratory syncytial virus (RSV) cause lower respiratory infections. The virus fusion (F) glycoprotein promotes membrane fusion by refolding from a metastable pre-fusion to a stable post-fusion conformation. F is also a major target of the neutralizing antibody response. Here we show that a potently neutralizing anti-HMPV antibody (DS7) binds a structurally invariant domain of F, identifying a new epitope that could be targeted in vaccine development. 2012-03-04 /pmc/articles/PMC3546531/ /pubmed/22388735 http://dx.doi.org/10.1038/nsmb.2250 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Wen, Xiaolin
Krause, Jens C.
Leser, George P.
Cox, Reagan G.
Lamb, Robert A.
Williams, John
Crowe, James E.
Jardetzky, Theodore S.
Structure of the Human Metapneumovirus Fusion Protein with Neutralizing Antibody Identifies a Pneumovirus Antigenic Site
title Structure of the Human Metapneumovirus Fusion Protein with Neutralizing Antibody Identifies a Pneumovirus Antigenic Site
title_full Structure of the Human Metapneumovirus Fusion Protein with Neutralizing Antibody Identifies a Pneumovirus Antigenic Site
title_fullStr Structure of the Human Metapneumovirus Fusion Protein with Neutralizing Antibody Identifies a Pneumovirus Antigenic Site
title_full_unstemmed Structure of the Human Metapneumovirus Fusion Protein with Neutralizing Antibody Identifies a Pneumovirus Antigenic Site
title_short Structure of the Human Metapneumovirus Fusion Protein with Neutralizing Antibody Identifies a Pneumovirus Antigenic Site
title_sort structure of the human metapneumovirus fusion protein with neutralizing antibody identifies a pneumovirus antigenic site
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3546531/
https://www.ncbi.nlm.nih.gov/pubmed/22388735
http://dx.doi.org/10.1038/nsmb.2250
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