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Direct Observation of Membrane Insertion by Enveloped Virus Matrix Proteins by Phosphate Displacement

Enveloped virus release is driven by poorly understood proteins that are functional analogs of the coat protein assemblies that mediate intracellular vesicle trafficking. We used differential electron density mapping to detect membrane integration by membrane-bending proteins from five virus familie...

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Detalles Bibliográficos
Autores principales: Neuman, Benjamin W., Kiss, Gabriella, Al-Mulla, Hawaa M. N., Dokland, Terje, Buchmeier, Michael J., Weikl, Thomas, Schley, David
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3585246/
https://www.ncbi.nlm.nih.gov/pubmed/23469104
http://dx.doi.org/10.1371/journal.pone.0057916
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author Neuman, Benjamin W.
Kiss, Gabriella
Al-Mulla, Hawaa M. N.
Dokland, Terje
Buchmeier, Michael J.
Weikl, Thomas
Schley, David
author_facet Neuman, Benjamin W.
Kiss, Gabriella
Al-Mulla, Hawaa M. N.
Dokland, Terje
Buchmeier, Michael J.
Weikl, Thomas
Schley, David
author_sort Neuman, Benjamin W.
collection PubMed
description Enveloped virus release is driven by poorly understood proteins that are functional analogs of the coat protein assemblies that mediate intracellular vesicle trafficking. We used differential electron density mapping to detect membrane integration by membrane-bending proteins from five virus families. This demonstrates that virus matrix proteins replace an unexpectedly large portion of the lipid content of the inner membrane face, a generalized feature likely to play a role in reshaping cellular membranes.
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spelling pubmed-35852462013-03-06 Direct Observation of Membrane Insertion by Enveloped Virus Matrix Proteins by Phosphate Displacement Neuman, Benjamin W. Kiss, Gabriella Al-Mulla, Hawaa M. N. Dokland, Terje Buchmeier, Michael J. Weikl, Thomas Schley, David PLoS One Research Article Enveloped virus release is driven by poorly understood proteins that are functional analogs of the coat protein assemblies that mediate intracellular vesicle trafficking. We used differential electron density mapping to detect membrane integration by membrane-bending proteins from five virus families. This demonstrates that virus matrix proteins replace an unexpectedly large portion of the lipid content of the inner membrane face, a generalized feature likely to play a role in reshaping cellular membranes. Public Library of Science 2013-02-28 /pmc/articles/PMC3585246/ /pubmed/23469104 http://dx.doi.org/10.1371/journal.pone.0057916 Text en © 2013 Neuman et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Neuman, Benjamin W.
Kiss, Gabriella
Al-Mulla, Hawaa M. N.
Dokland, Terje
Buchmeier, Michael J.
Weikl, Thomas
Schley, David
Direct Observation of Membrane Insertion by Enveloped Virus Matrix Proteins by Phosphate Displacement
title Direct Observation of Membrane Insertion by Enveloped Virus Matrix Proteins by Phosphate Displacement
title_full Direct Observation of Membrane Insertion by Enveloped Virus Matrix Proteins by Phosphate Displacement
title_fullStr Direct Observation of Membrane Insertion by Enveloped Virus Matrix Proteins by Phosphate Displacement
title_full_unstemmed Direct Observation of Membrane Insertion by Enveloped Virus Matrix Proteins by Phosphate Displacement
title_short Direct Observation of Membrane Insertion by Enveloped Virus Matrix Proteins by Phosphate Displacement
title_sort direct observation of membrane insertion by enveloped virus matrix proteins by phosphate displacement
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3585246/
https://www.ncbi.nlm.nih.gov/pubmed/23469104
http://dx.doi.org/10.1371/journal.pone.0057916
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