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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...

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Detalles Bibliográficos
Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cell Press 2017
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
Descripción
Sumario: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.