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Dynamin-2 Stabilizes the HIV-1 Fusion Pore with a Low Oligomeric State
One of the key research areas surrounding HIV-1 concerns the regulation of the fusion event that occurs between the virus particle and the host cell during entry. Even if it is universally accepted that the large GTPase dynamin-2 is important during HIV-1 entry, its exact role during the first steps...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cell Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5263234/ https://www.ncbi.nlm.nih.gov/pubmed/28076788 http://dx.doi.org/10.1016/j.celrep.2016.12.032 |
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author | Jones, Daniel M. Alvarez, Luis A. Nolan, Rory Ferriz, Margarita Sainz Urruela, Raquel Massana-Muñoz, Xènia Novak-Kotzer, Hila Dustin, Michael L. Padilla-Parra, Sergi |
author_facet | Jones, Daniel M. Alvarez, Luis A. Nolan, Rory Ferriz, Margarita Sainz Urruela, Raquel Massana-Muñoz, Xènia Novak-Kotzer, Hila Dustin, Michael L. Padilla-Parra, Sergi |
author_sort | Jones, Daniel M. |
collection | PubMed |
description | One of the key research areas surrounding HIV-1 concerns the regulation of the fusion event that occurs between the virus particle and the host cell during entry. Even if it is universally accepted that the large GTPase dynamin-2 is important during HIV-1 entry, its exact role during the first steps of HIV-1 infection is not well characterized. Here, we have utilized a multidisciplinary approach to study the DNM2 role during fusion of HIV-1 in primary resting CD4 T and TZM-bl cells. We have combined advanced light microscopy and functional cell-based assays to experimentally assess the role of dynamin-2 during these processes. Overall, our data suggest that dynamin-2, as a tetramer, might help to establish hemi-fusion and stabilizes the pore during HIV-1 fusion. |
format | Online Article Text |
id | pubmed-5263234 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Cell Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-52632342017-01-30 Dynamin-2 Stabilizes the HIV-1 Fusion Pore with a Low Oligomeric State Jones, Daniel M. Alvarez, Luis A. Nolan, Rory Ferriz, Margarita Sainz Urruela, Raquel Massana-Muñoz, Xènia Novak-Kotzer, Hila Dustin, Michael L. Padilla-Parra, Sergi Cell Rep Article One of the key research areas surrounding HIV-1 concerns the regulation of the fusion event that occurs between the virus particle and the host cell during entry. Even if it is universally accepted that the large GTPase dynamin-2 is important during HIV-1 entry, its exact role during the first steps of HIV-1 infection is not well characterized. Here, we have utilized a multidisciplinary approach to study the DNM2 role during fusion of HIV-1 in primary resting CD4 T and TZM-bl cells. We have combined advanced light microscopy and functional cell-based assays to experimentally assess the role of dynamin-2 during these processes. Overall, our data suggest that dynamin-2, as a tetramer, might help to establish hemi-fusion and stabilizes the pore during HIV-1 fusion. Cell Press 2017-01-10 /pmc/articles/PMC5263234/ /pubmed/28076788 http://dx.doi.org/10.1016/j.celrep.2016.12.032 Text en © 2017 University of Oxford http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Jones, Daniel M. Alvarez, Luis A. Nolan, Rory Ferriz, Margarita Sainz Urruela, Raquel Massana-Muñoz, Xènia Novak-Kotzer, Hila Dustin, Michael L. Padilla-Parra, Sergi Dynamin-2 Stabilizes the HIV-1 Fusion Pore with a Low Oligomeric State |
title | Dynamin-2 Stabilizes the HIV-1 Fusion Pore with a Low Oligomeric State |
title_full | Dynamin-2 Stabilizes the HIV-1 Fusion Pore with a Low Oligomeric State |
title_fullStr | Dynamin-2 Stabilizes the HIV-1 Fusion Pore with a Low Oligomeric State |
title_full_unstemmed | Dynamin-2 Stabilizes the HIV-1 Fusion Pore with a Low Oligomeric State |
title_short | Dynamin-2 Stabilizes the HIV-1 Fusion Pore with a Low Oligomeric State |
title_sort | dynamin-2 stabilizes the hiv-1 fusion pore with a low oligomeric state |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5263234/ https://www.ncbi.nlm.nih.gov/pubmed/28076788 http://dx.doi.org/10.1016/j.celrep.2016.12.032 |
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