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Viral membrane fusion
Infection by viruses having lipid-bilayer envelopes proceeds through fusion of the viral membrane with a membrane of the target cell. Viral 'fusion proteins' facilitate this process. They vary greatly in structure, but all seem to have a common mechanism of action, in which a ligand-trigge...
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Formato: | Texto |
Lenguaje: | English |
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Nature Publishing Group US
2008
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2517140/ https://www.ncbi.nlm.nih.gov/pubmed/18596815 http://dx.doi.org/10.1038/nsmb.1456 |
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author | Harrison, Stephen C |
author_facet | Harrison, Stephen C |
author_sort | Harrison, Stephen C |
collection | PubMed |
description | Infection by viruses having lipid-bilayer envelopes proceeds through fusion of the viral membrane with a membrane of the target cell. Viral 'fusion proteins' facilitate this process. They vary greatly in structure, but all seem to have a common mechanism of action, in which a ligand-triggered, large-scale conformational change in the fusion protein is coupled to apposition and merger of the two bilayers. We describe three examples—the influenza virus hemagglutinin, the flavivirus E protein and the vesicular stomatitis virus G protein—in some detail, to illustrate the ways in which different structures have evolved to implement this common mechanism. Fusion inhibitors can be effective antiviral agents. |
format | Text |
id | pubmed-2517140 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Nature Publishing Group US |
record_format | MEDLINE/PubMed |
spelling | pubmed-25171402009-01-01 Viral membrane fusion Harrison, Stephen C Nat Struct Mol Biol Article Infection by viruses having lipid-bilayer envelopes proceeds through fusion of the viral membrane with a membrane of the target cell. Viral 'fusion proteins' facilitate this process. They vary greatly in structure, but all seem to have a common mechanism of action, in which a ligand-triggered, large-scale conformational change in the fusion protein is coupled to apposition and merger of the two bilayers. We describe three examples—the influenza virus hemagglutinin, the flavivirus E protein and the vesicular stomatitis virus G protein—in some detail, to illustrate the ways in which different structures have evolved to implement this common mechanism. Fusion inhibitors can be effective antiviral agents. Nature Publishing Group US 2008-07-03 2008 /pmc/articles/PMC2517140/ /pubmed/18596815 http://dx.doi.org/10.1038/nsmb.1456 Text en © Nature Publishing Group 2008 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Article Harrison, Stephen C Viral membrane fusion |
title | Viral membrane fusion |
title_full | Viral membrane fusion |
title_fullStr | Viral membrane fusion |
title_full_unstemmed | Viral membrane fusion |
title_short | Viral membrane fusion |
title_sort | viral membrane fusion |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2517140/ https://www.ncbi.nlm.nih.gov/pubmed/18596815 http://dx.doi.org/10.1038/nsmb.1456 |
work_keys_str_mv | AT harrisonstephenc viralmembranefusion |