Dynamin-2 Stabilizes the HIV-1 Fusion Pore with a Low Oligomeric State

Publication date: 10 January 2017
Source:Cell Reports, Volume 18, Issue 2
Author(s): Daniel M. Jones, Luis A. Alvarez, Rory Nolan, Margarita Ferriz, Raquel Sainz Urruela, Xènia Massana-Muñoz, Hila Novak-Kotzer, Michael L. Dustin, Sergi Padilla-Parra
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.

Graphical abstract

Teaser

Regulation of HIV-1 fusion is one of the research areas of intense interest. Here, Jones et al. show that the large GTPase dynamin-2 (DNM2) forms a tetramer that acts to stabilize the HIV fusion pore.


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