Human immunodeficiency virus type-1 (HIV-1), the causative agent of AIDS, is blamed for over 20 million deaths and is poised to claim 2-3 million lives a year in the absence of efficient therapeutic intervention. HIV-1 encodes a polypeptide called Gag that is capable of forming virus-like particles (VLP) in vitro in the absence of other cellular or viral constituents. HIV-1 Gag polyprotein is routed to multivesicular bodies (MVB) and subsequently to the plasma membrane for assembly through discrete, sequential interactions with cellular transport pathways.
We are interested in the underlying structural basis by which retroviral Gag polyproteins interact with cellular constituents during the virus replication cycle. A major component of my research is directed towards understanding key protein-protein and protein-membrane interactions that are critical for retroviral assembly. The identification of cellular factors interacting with Gag has gained a new momentum in the last few years. We employ a set of biochemical, biophysical and structural biology tools to identify the molecular mechanisms governing HIV-1 Gag intracellular trafficking and subsequent assembly on the PM.
Our studies will offer a better understanding of how HIV-1 Gag protein interact with the host cell to facilitate trafficking and assembly, which may aid in the development of new drugs for the treatment of HIV.
