Abstract
SummaryOne 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.
Highlights
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
A virion packaging Vpr-beta-lactamase assay (BlaM) is liberated into the cytoplasm of a target cell and a Forster resonance energy transfer (FRET) substrate (CCF2) is cleaved and the fluorescence profile altered (Figure 1A)
Previous reports have shown that the HIV envelope, but not the VSV-G protein is capable of mediating HIV infection of resting CD4 T cells (Agosto et al, 2009)
Summary
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. As an alternative to plasma membrane fusion, clathrin-mediated endocytosis (CME) allows viruses to cross the cell plasma membrane harbored within endocytic vesicles, followed by a fusion event between the membranes of the virus and the endosome. This process requires precise signaling events to initiate the process, but to ensure that fusion occurs prior to degradation of the virus particle within the increasingly toxic environment of the endolysosomal machinery (Stein et al, 1987)
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