基质在HIV-1包膜糖蛋白掺入中的作用。
The role of matrix in HIV-1 envelope glycoprotein incorporation.
作者信息
Tedbury Philip R, Freed Eric O
机构信息
Virus-Cell Interaction Section, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702-1201, USA.
出版信息
Trends Microbiol. 2014 Jul;22(7):372-8. doi: 10.1016/j.tim.2014.04.012. Epub 2014 Jun 2.
Abstract
Incorporation of the viral envelope (Env) glycoprotein is a critical requirement for the production of infectious HIV-1 particles. It has long been appreciated that the matrix (MA) domain of the Gag polyprotein and the cytoplasmic tail of Env are central players in the process of Env incorporation, but the precise mechanisms have been elusive. Several recent developments have thrown light on the contributions of both proteins, prompting a re-evaluation of the role of MA during Env incorporation. The two domains appear to play distinct but complementary roles, with the cytoplasmic tail of Env responsible for directing Env to the site of assembly and the matrix domain accommodating the cytoplasmic tail of Env in the Gag lattice.
摘要
病毒包膜（Env）糖蛋白的整合是产生具有传染性的HIV-1颗粒的关键条件。长期以来人们一直认识到，Gag多聚蛋白的基质（MA）结构域和Env的胞质尾在Env整合过程中起着核心作用，但具体机制一直难以捉摸。最近的一些进展揭示了这两种蛋白质的作用，促使人们重新评估MA在Env整合过程中的作用。这两个结构域似乎发挥着不同但互补的作用，Env的胞质尾负责将Env引导至组装位点，而基质结构域则在Gag晶格中容纳Env的胞质尾。
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