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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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
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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. |
format | Online Article Text |
id | pubmed-3585246 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
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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