Abstract

HIV Viral protein R (Vpr) is a multifunctional accessory protein which plays a role in nuclear import of the pre-integration complex, transactivation of HIV LTR promoter, cell cycle arrest, and apoptosis during HIV infection. R77Q is an HIV Vpr mutant which is associated with long-term non-progressor phenotypes, and which has previously been connected to higher levels of apoptosis compared to wild type Vpr in vitro. There are observable differences in host binding partners with HIV Vpr between wild type and R77Q strains as shown via coimmunoprecipitation and mass spectrometry. In one run R77Q samples showed binding to histone 1.2, 1.3, 1.5, 1.10 and histone 4, as well as Adhesion G-protein coupled receptor V1, Polyubiquitin-C, and small ribosomal subunit protein uS9. In the WT samples only complement component C7 was identified as a significantly bound protein. In a second experimental run, histone type 2-C tubulin alpha-4A and 1A chains, gamma-enolase, phosphoglycerate mutase 1, dihydropyrimidinase-related protein 2, malate dehydrogenase cytoplasmic and mitochondrial, 14-3-3 protein ζ /Δ and beta/alpha, and pyruvate kinase PKM were identified to have significantly more binding to R77Q Vpr than wild type. In a literature search, most of these proteins were identified to have connections with HIV infection, Vpr, cell cycle regulation, or apoptosis pathways.

Degree

College and Department

Life Sciences; Microbiology and Molecular Biology

Rights

https://lib.byu.edu/about/copyright/