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Association of Influenza Virus Proteins with Membrane Rafts

Assembly and budding of influenza virus proceeds in the viral budozone, a domain in the plasma membrane with characteristics of cholesterol/sphingolipid-rich membrane rafts. The viral transmembrane glycoproteins hemagglutinin (HA) and neuraminidase (NA) are intrinsically targeted to these domains, w...

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Detalles Bibliográficos
Autores principales: Veit, Michael, Thaa, Bastian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3265303/
https://www.ncbi.nlm.nih.gov/pubmed/22312341
http://dx.doi.org/10.1155/2011/370606
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author Veit, Michael
Thaa, Bastian
author_facet Veit, Michael
Thaa, Bastian
author_sort Veit, Michael
collection PubMed
description Assembly and budding of influenza virus proceeds in the viral budozone, a domain in the plasma membrane with characteristics of cholesterol/sphingolipid-rich membrane rafts. The viral transmembrane glycoproteins hemagglutinin (HA) and neuraminidase (NA) are intrinsically targeted to these domains, while M2 is seemingly targeted to the edge of the budozone. Virus assembly is orchestrated by the matrix protein M1, binding to all viral components and the membrane. Budding progresses by protein- and lipid-mediated membrane bending and particle scission probably mediated by M2. Here, we summarize the experimental evidence for this model with emphasis on the raft-targeting features of HA, NA, and M2 and review the functional importance of raft domains for viral protein transport, assembly and budding, environmental stability, and membrane fusion.
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spelling pubmed-32653032012-02-06 Association of Influenza Virus Proteins with Membrane Rafts Veit, Michael Thaa, Bastian Adv Virol Review Article Assembly and budding of influenza virus proceeds in the viral budozone, a domain in the plasma membrane with characteristics of cholesterol/sphingolipid-rich membrane rafts. The viral transmembrane glycoproteins hemagglutinin (HA) and neuraminidase (NA) are intrinsically targeted to these domains, while M2 is seemingly targeted to the edge of the budozone. Virus assembly is orchestrated by the matrix protein M1, binding to all viral components and the membrane. Budding progresses by protein- and lipid-mediated membrane bending and particle scission probably mediated by M2. Here, we summarize the experimental evidence for this model with emphasis on the raft-targeting features of HA, NA, and M2 and review the functional importance of raft domains for viral protein transport, assembly and budding, environmental stability, and membrane fusion. Hindawi Publishing Corporation 2011 2011-07-25 /pmc/articles/PMC3265303/ /pubmed/22312341 http://dx.doi.org/10.1155/2011/370606 Text en Copyright © 2011 M. Veit and B. Thaa. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Veit, Michael
Thaa, Bastian
Association of Influenza Virus Proteins with Membrane Rafts
title Association of Influenza Virus Proteins with Membrane Rafts
title_full Association of Influenza Virus Proteins with Membrane Rafts
title_fullStr Association of Influenza Virus Proteins with Membrane Rafts
title_full_unstemmed Association of Influenza Virus Proteins with Membrane Rafts
title_short Association of Influenza Virus Proteins with Membrane Rafts
title_sort association of influenza virus proteins with membrane rafts
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3265303/
https://www.ncbi.nlm.nih.gov/pubmed/22312341
http://dx.doi.org/10.1155/2011/370606
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