Open AccessDynamin-2 Stabilizes the HIV-1 Fusion Pore with a Low Oligomeric State
Author(s) -
Daniel M. Jones,
Luis Álvarez,
Rory Nolan,
Margarita Ferriz,
Raquel Sainz-Urruela,
Xènia Massana-Muñoz,
Hila NovakKotzer,
Michael L. Dustin,
Sergi PadillaParra
Publication year - 2017
Publication title -
cell reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.264
H-Index - 154
eISSN - 2639-1856
pISSN - 2211-1247
DOI - 10.1016/j.celrep.2016.12.032
Subject(s) - dynamin , gtpase , fusion , microbiology and biotechnology , human immunodeficiency virus (hiv) , virology , fusion mechanism , chemistry , biology , lipid bilayer fusion , virus , biophysics , endocytosis , cell , biochemistry , linguistics , philosophy
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom