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Retroviral matrix and lipids, the intimate interaction

Retroviruses are enveloped viruses that assemble on the inner leaflet of cellular membranes. Improving biophysical techniques has recently unveiled many molecular aspects of the interaction between the retroviral structural protein Gag and the cellular membrane lipids. This interaction is driven by...

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Detalles Bibliográficos
Autores principales: Hamard-Peron, Elise, Muriaux, Delphine
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3059298/
https://www.ncbi.nlm.nih.gov/pubmed/21385335
http://dx.doi.org/10.1186/1742-4690-8-15
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author Hamard-Peron, Elise
Muriaux, Delphine
author_facet Hamard-Peron, Elise
Muriaux, Delphine
author_sort Hamard-Peron, Elise
collection PubMed
description Retroviruses are enveloped viruses that assemble on the inner leaflet of cellular membranes. Improving biophysical techniques has recently unveiled many molecular aspects of the interaction between the retroviral structural protein Gag and the cellular membrane lipids. This interaction is driven by the N-terminal matrix domain of the protein, which probably undergoes important structural modifications during this process, and could induce membrane lipid distribution changes as well. This review aims at describing the molecular events occurring during MA-membrane interaction, and pointing out their consequences in terms of viral assembly. The striking conservation of the matrix membrane binding mode among retroviruses indicates that this particular step is most probably a relevant target for antiviral research.
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spelling pubmed-30592982011-03-17 Retroviral matrix and lipids, the intimate interaction Hamard-Peron, Elise Muriaux, Delphine Retrovirology Review Retroviruses are enveloped viruses that assemble on the inner leaflet of cellular membranes. Improving biophysical techniques has recently unveiled many molecular aspects of the interaction between the retroviral structural protein Gag and the cellular membrane lipids. This interaction is driven by the N-terminal matrix domain of the protein, which probably undergoes important structural modifications during this process, and could induce membrane lipid distribution changes as well. This review aims at describing the molecular events occurring during MA-membrane interaction, and pointing out their consequences in terms of viral assembly. The striking conservation of the matrix membrane binding mode among retroviruses indicates that this particular step is most probably a relevant target for antiviral research. BioMed Central 2011-03-07 /pmc/articles/PMC3059298/ /pubmed/21385335 http://dx.doi.org/10.1186/1742-4690-8-15 Text en Copyright ©2011 Hamard-Peron and Muriaux; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
Hamard-Peron, Elise
Muriaux, Delphine
Retroviral matrix and lipids, the intimate interaction
title Retroviral matrix and lipids, the intimate interaction
title_full Retroviral matrix and lipids, the intimate interaction
title_fullStr Retroviral matrix and lipids, the intimate interaction
title_full_unstemmed Retroviral matrix and lipids, the intimate interaction
title_short Retroviral matrix and lipids, the intimate interaction
title_sort retroviral matrix and lipids, the intimate interaction
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3059298/
https://www.ncbi.nlm.nih.gov/pubmed/21385335
http://dx.doi.org/10.1186/1742-4690-8-15
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