Effects of human immunodeficiency virus type 1 transframe protein p6*mutations on viral protease-mediated Gag processing
Effects of human immunodeficiency virus type 1 transframe protein p6*mutations on viral protease-mediated Gag processing
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DOI：
10.1099/vir.0.81601-0
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发表时间：
2006-07-01
影响因子：
3.8
通讯作者：
Wang, Chin-Tien
中科院分区：
文献类型：
--
作者：
Chiu, Hsu-Chen;Wang, Fu-Der;Wang, Chin-Tien
由病毒编码的蛋白酶（PR）介导的人类免疫缺陷病毒（HIV）颗粒的蛋白水解加工对于病毒感染性是必需的。pol编码序列与gag编码序列部分重叠，并被翻译为Gag-Pol多蛋白前体。在Gag-Pol中，C-末端p6（gag）结构域被称为p6* 的跨框肽取代，其将Gag核衣壳结构域与PR分离。先前的几项体外研究将PR抑制调节功能归因于p6*。这里，证明了当与HIV-1 Gag前体共表达时，缺乏p6* 的HIV-1 Gag-Pol被有效地掺入病毒体中。然而，释放的病毒粒子没有得到适当的处理，并显示出大大降低的病毒感染性。这表明p6* 在PR介导的病毒颗粒成熟过程中是必不可少的。
The proteolytic processing of human immunodeficiency virus (HIV) particles mediated by the viral po/-encoded protease (PR) is essential for viral infectivity. The pol coding sequence partially overlaps with the gag coding sequence and is translated as a Gag-Pol polyprotein precursor. Within Gag-Pol, the C-terminal p6(gag) domain is replaced by a transframe peptide referred to as p6*, which separates the Gag nucleocapsid domain from PR. Several previous in vitro studies have ascribed a PR-suppression regulatory function to p6*. Here, it was demonstrated that an HIV-1 Gag-Pol lacking p6* is efficiently incorporated into virions when coexpressed with HIV-1 Gag precursor. However, the released virions are not processed appropriately and show a greatly reduced viral infectivity. This suggests that the p6* is indispensable during the process of PR-mediated virus particle maturation.