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Molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies

A key step in infections by enveloped viruses, such as influenza, is the fusion between the viral envelope and the host cell membrane, which allows the virus to insert its genetic material into the host cell and replicate. The influenza virus fusion process is promoted by hemagglutinin (HA), a glyco...

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Detalles Bibliográficos
Autores principales: Lousa, Diana, Soares, Cláudio M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8634857/
https://www.ncbi.nlm.nih.gov/pubmed/34710289
http://dx.doi.org/10.1002/2211-5463.13323
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author Lousa, Diana
Soares, Cláudio M.
author_facet Lousa, Diana
Soares, Cláudio M.
author_sort Lousa, Diana
collection PubMed
description A key step in infections by enveloped viruses, such as influenza, is the fusion between the viral envelope and the host cell membrane, which allows the virus to insert its genetic material into the host cell and replicate. The influenza virus fusion process is promoted by hemagglutinin (HA), a glycoprotein that contains three identical monomers composed of two polypeptide chains (HA1 and HA2). Early studies on this protein revealed that HA‐mediated fusion involves the insertion of the HA2 N‐terminal segment into the host membrane and that this segment, known as the fusion peptide, is a key player in the fusion process. This mini‐review highlights the main findings that have been obtained by experimental and computational studies on the HA fusion peptide, which give us a glimpse of its mode of action.
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spelling pubmed-86348572021-12-08 Molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies Lousa, Diana Soares, Cláudio M. FEBS Open Bio Reviews A key step in infections by enveloped viruses, such as influenza, is the fusion between the viral envelope and the host cell membrane, which allows the virus to insert its genetic material into the host cell and replicate. The influenza virus fusion process is promoted by hemagglutinin (HA), a glycoprotein that contains three identical monomers composed of two polypeptide chains (HA1 and HA2). Early studies on this protein revealed that HA‐mediated fusion involves the insertion of the HA2 N‐terminal segment into the host membrane and that this segment, known as the fusion peptide, is a key player in the fusion process. This mini‐review highlights the main findings that have been obtained by experimental and computational studies on the HA fusion peptide, which give us a glimpse of its mode of action. John Wiley and Sons Inc. 2021-11-08 /pmc/articles/PMC8634857/ /pubmed/34710289 http://dx.doi.org/10.1002/2211-5463.13323 Text en © 2021 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Reviews
Lousa, Diana
Soares, Cláudio M.
Molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies
title Molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies
title_full Molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies
title_fullStr Molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies
title_full_unstemmed Molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies
title_short Molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies
title_sort molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8634857/
https://www.ncbi.nlm.nih.gov/pubmed/34710289
http://dx.doi.org/10.1002/2211-5463.13323
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