Lee Y H, Schwartz M D, Panganiban A T
McArdle Laboratory for Cancer Research, University of Wisconsin Medical School, 1400 University Avenue, Madison, Wisconsin 53706, USA.
Virology. 1997 Oct 13;237(1):46-55. doi: 10.1006/viro.1997.8711.
HIV-1 viral protein U (Vpu) facilitates virus particle release. To determine whether Gag is sufficient for generation of a target for Vpu-mediated particle release, we expressed HIV-1 Gag protein in the absence of the other viral genes. The resulting particles were still Vpu responsive. Mutational analysis of Gag indicated that the matrix domain (MA) is required for Vpu responsiveness. However, additional mutations in other domains of Gag, which affect the formation of stable virus particles, also abrogate Vpu responsiveness on total Gag release. Coexpression of the wild-type gag gene and a gag mutant lacking the MA domain renders the MA- mutant Vpu responsive. This indicates that Gag molecules lacking MA are still incorporated into particles through association with wild-type Gag molecules and that the resulting composite particles are sufficient for Vpu-mediated exit.
HIV-1病毒蛋白U（Vpu）促进病毒颗粒释放。为了确定Gag对于生成Vpu介导的颗粒释放靶点是否足够，我们在没有其他病毒基因的情况下表达了HIV-1 Gag蛋白。产生的颗粒仍然对Vpu有反应。对Gag的突变分析表明，基质结构域（MA）是Vpu反应所必需的。然而，Gag其他结构域中的额外突变会影响稳定病毒颗粒的形成，这也会消除Vpu对总Gag释放的反应。野生型gag基因与缺乏MA结构域的gag突变体共表达，使MA突变体对Vpu有反应。这表明缺乏MA的Gag分子仍通过与野生型Gag分子结合而被整合到颗粒中，并且产生的复合颗粒足以介导Vpu介导的释放。
