Cargando…
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...
Autores principales: | , |
---|---|
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 |
_version_ | 1782200402335236096 |
---|---|
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. |
format | Text |
id | pubmed-3059298 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT hamardperonelise retroviralmatrixandlipidstheintimateinteraction AT muriauxdelphine retroviralmatrixandlipidstheintimateinteraction |