Sato A, Yoshimoto J, Isaka Y, Miki S, Suyama A, Adachi A, Hayami M, Fujiwara T, Yoshie O
Shionogi Institute for Medical Science, Osaka, Japan.
Virology. 1996 Jun 1;220(1):208-12. doi: 10.1006/viro.1996.0302.
Vpr is one of the auxiliary proteins of HIV-1 and is selectively incorporated into the virion by a process involving the C-terminal p6 portion of the Gag precursor Pr55. Vpr and the matrix protein p17 are the components of the viral preintegration complex and appear to play important roles in the nuclear transport of proviral DNA in nondividing cells. In the present study, we have demonstrated by coimmunoprecipitation experiments that Vpr associates with matrix protein p17 but not with capsid protein p24 within the HIV-1 virion. Experiments employing the yeast two-hybrid GAL4 assay for protein-protein interactions also demonstrated a direct association between Vpr and the C-terminal region of matrix protein p17. Association of Vpr and the matrix protein p17 within the mature virion is consistent with their collaborative role in the nuclear transportation of the viral preintegration complex in nondividing cells such as macrophages.
Vpr是HIV-1的辅助蛋白之一,通过一个涉及Gag前体Pr55的C末端p6部分的过程被选择性地整合到病毒颗粒中。Vpr和基质蛋白p17是病毒整合前复合物的组成部分,似乎在非分裂细胞中前病毒DNA的核运输中发挥重要作用。在本研究中,我们通过免疫共沉淀实验证明,在HIV-1病毒颗粒内,Vpr与基质蛋白p17相关联,但与衣壳蛋白p24不相关。采用酵母双杂交GAL4分析蛋白质-蛋白质相互作用的实验也证明了Vpr与基质蛋白p17的C末端区域之间存在直接关联。成熟病毒颗粒内Vpr与基质蛋白p17的关联与其在巨噬细胞等非分裂细胞中病毒整合前复合物的核运输中的协同作用一致。