Identification of residues in the N-terminal acidic domain of HIV-1 Vpr essential for virion incorporation.
Identification of residues in the N-terminal acidic domain of HIV-1 Vpr essential for virion incorporation.
复制标题
鉴定 HIV-1 Vpr N 端酸性结构域中对于病毒粒子掺入至关重要的残基。
DOI：
10.1006/viro.1995.1081
复制
发表时间：
1995
期刊：
影响因子：
--
通讯作者：
Srinivasan,A
中科院分区：
文献类型：
--
作者：
Mahalingam,S;Khan,SA;Jabbar,MA;Monken,CE;Collman,RG;Srinivasan,A
Vpr是由HIV-1基因组编码的辅助蛋白之一，并选择性地掺入病毒颗粒中。已经表明，Vpr掺入病毒颗粒中仅需要核心蛋白Gag。为了鉴定Vpr的结构域，其对于掺入HIV-1病毒体是必需的，进行了Vpr的位点特异性诱变。在N-末端结构域中高度保守的酸性残基（氨基酸位置17-34）的突变消除了病毒体掺入。这些突变破坏了Vpr序列中高度保守的预测的两亲性α-螺旋结构。与此相反，保守的半胱氨酸（Cys 76），碱性结构域（Arg 87和Lys 95），和其他残基（Gln 65）的改变并没有损害Vpr的掺入到病毒样颗粒的HIV-1 Gag指导。这里提出的结果表明，蛋白质-蛋白质相互作用介导的Vpr的推定的螺旋结构域可能参与其纳入病毒颗粒。
Vpr is one of the auxiliary proteins encoded by the HIV-1 genome and is selectively incorporated into the virus particle. It has been shown that Vpr incorporation in the virus particle requires only the core protein Gag. In an effort to identify the domains of Vpr which are essential for incorporation into the HIV-1 virion, site-specific mutagenesis of vpr was carried out. Mutation of the highly conserved acidic residues in the N-terminal domain (amino acid positions 17-34) eliminated virion incorporation. These mutations disrupt a predicted amphipathic alpha-helical structure that is highly conserved among Vpr sequences. In contrast, alterations of the conserved cysteine (Cys76), basic domain (Arg87 and Lys95), and other residues (Gln65) did not impair the incorporation of Vpr into virus-like particles directed by HIV-1 Gag. The results presented here suggest that protein-protein interactions mediated through the putative helical domain of Vpr may participate in its incorporation into the virus particle.