Interaction of HIV-1 Viral protein R and p6

Human immunodeficiency virus type 1 (HIV-1) Gag polyprotein (Gag pp) mediates the assembly and release of virus-like particles from an infected cell membrane. During the HIV-1 life cycle, the Gag pp C-terminal p6 is cleaved and presents a disordered structure in aqueous solution. The p6 domain has been recognized as the docking site for viral binding partners, such as Viral Protein R (Vpr). The adjacency of the cellular membrane can prompt p6 interaction with Vpr, stabilizing its folding. Aim of this proposal is to investigate the interaction between p6 and Vpr in solution and whether it is affected in proximity of different phospholipid and glycolipid surfaces. This study may elucidate p6 functional role in connection with spreading events in the viral life cycle.