Study reveals how a Rab protein controls HIV-1 replication
Rockefeller University Press
4-May-2015 - HIV-1 replication requires the coordinated movement of the virus's components toward the plasma membrane of an immune cell, where the virions are assembled and ultimately released. A study in The Journal of Cell Biology reveals
how a Rab protein that controls intracellular trafficking supports HIV-1 assembly by promoting high
levels of an important membrane lipid.
New HIV-1 particles assemble at specialized sites in the plasma membrane that are enriched in
PIP 2 , a phospholipid component of the membrane that recruits a viral protein called Pr55 Gag
(Gag) that directs HIV-1 assembly. Because certain cell secretion pathways have been suggested
to be required for this process, University of Buenos Aires researcher Matías Ostrowski
and colleagues investigated whether a role might be played by Rab27a, a protein that guides
delivery of membrane-bound compartments called endosomes to the plasma membrane.
Ostrowski and colleagues found that viral replication was impaired in immune cells lacking Rab27a.
These cells showed reduced levels of PIP 2 at the plasma membrane and thus failed to recruit Gag to
form viral assembly sites. The researchers determined that Rab27a boosted PIP 2 production at the
plasma membrane by controlling the endosomal delivery of an enzyme that is necessary for
production of the phospholipid to the cell periphery.
Ostrowski believes that these results open a path to investigate whether manipulating endosomal
traffic could be a new target for anti-HIV-1 therapies.
Pereyra Gerber, P., et al. 2015. J. Cell Biol. doi:10.1083/jcb.201409082
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Rita Sullivan King
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