Dynamin-2 Stabilizes the HIV-1 Fusion Pore with a Low Oligomeric State.
Jones DM., Alvarez LA., Nolan R., Ferriz M., Sainz Urruela R., Massana-Muñoz X., Novak-Kotzer H., Dustin ML., Padilla-Parra S.
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.