The Lingappa Lab's approach to understanding HIV assembly:

The central hypothesis underlying our approach is that HIV uses host proteins to co-ordinate, catalyze, and/or chaperone the events of virus assembly. Others have shown that purified recombinant Gag proteins can spontaneously assemble in buffer when Gag is present at high concentrations, in the absence of cellular proteins or organelles. However, these spontaneous assembly systems do not reconstitute the link between translation and post-translation events that occurs in vivo.  Moreover, they do not mimic the environment of the eukaryotic cytoplasm. This is problematic because efficient capsid assembly in the complicated environment of the eukaryotic cytoplasm may require cellular proteins to link translation to post-translational events and promote targeting and assembly of newly-synthesized Gag proteins. Indeed, the role of cellular proteins in promoting HIV budding and release has been elegantly demonstrated by a number of groups (see Morita and Sundquist, 2004; Freed, 2004 for reviews). Similarly, cellular proteins may be critical for facilitating efficient Gag assembly and encapsidation.

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