Li M S, Garcia-Asua G, Bhattacharyya U, Mascagni P, Austen B M, Roberts M M
Department of Medical Microbiology, St. George's Hospital Medical School, University of London, U.K.
Biochem Biophys Res Commun. 1996 Jan 5;218(1):352-5. doi: 10.1006/bbrc.1996.0061.
The Vpr protein of human immunodeficiency virus type 1 (HIV-1) is incorporated into the virion by the Gag polyprotein precursor Pr55gag. The importance of the p6gag sequence at the C-terminal end of Pr55gag has a crucial role in Vpr incorporation. To identify the Gag sequences directly involved in Vpr binding, we compared the Vpr binding affinities of the 71 amino acid nucleocapsid protein p7, the C-terminal peptide (35-71) p7C and p6gag by affinity chromatography. p7 and p7C have the strongest Vpr binding activities compared to p6gag. These results suggest that the nucleocapsid protein and its C-terminal domain may be important for the incorporation of Vpr into the mature HIV-1 virion and the subsequent localisation of viral nucleic acid to the cell nucleus by Vpr.
人类免疫缺陷病毒1型（HIV-1）的Vpr蛋白通过Gag多聚蛋白前体Pr55gag整合到病毒粒子中。Pr55gag C末端的p6gag序列的重要性在Vpr整合中起关键作用。为了鉴定直接参与Vpr结合的Gag序列，我们通过亲和色谱比较了71个氨基酸的核衣壳蛋白p7、C末端肽（35-71）p7C和p6gag的Vpr结合亲和力。与p6gag相比，p7和p7C具有最强的Vpr结合活性。这些结果表明，核衣壳蛋白及其C末端结构域对于Vpr整合到成熟的HIV-1病毒粒子中以及随后Vpr将病毒核酸定位到细胞核可能很重要。
