Biochemical mechanism of HIV-I Vpr function. Specific interaction with a cellular protein.

摘要: vpr is an accessory gene of human immunodeficiency virus I (HIV-I). Although unnecessary for viral replication in T cell lines, growing evidence suggests that it essential monocytes/macrophages and vivo. We expressed HIV-I Escherichia coli purified Vpr by affinity chromatography. In a coprecipitation assay, the interacted specifically with cellular protein designated as Vpr-interacting protein, or RIP. Mutational analysis suggested this interaction required domain rich leucine/isoleucine residues highly conserved between SIVmac Vprs. During transient expression mammalian cells, was localized nucleus. However, mutational failed to identify typical nuclear localization signal basic amino acid residues. Instead, seemed correlate Mutations C-terminal 20-amino region containing cryptic did not abolish RIP, whereas point mutations leucine/isoleucine-rich abolished RIP rendered unstable during expression. These results suggest may be involved function.