Kaplan Andrew H
Department of Medicine, Microbiology & Immunology, University of North Carolina, Chapel Hill, North Carolina, USA.
AIDS Rev. 2002 Apr-Jun;4(2):104-11.
The core particle of HIV-1 assembles at the membrane of the host cell as the virus buds from the surface. The structural proteins and enzymes that comprise the core are translated as part of two polyprotein precursors, Gag and GagPol. The Gag precursor contains the structural proteins of the core and is both necessary and sufficient for directing particle assembly and budding. Over the past few years, significant progress has been made in our understanding of the interactions that drive particle assembly. Specifically, determinants within the Gag precursor that direct membrane association, Gag-Gag interactions and particle budding have been identified and partially characterized. Subdomains of the host cell membrane that favor particle assembly and budding have also been described. Finally, a potential role for cellular processes in mediating the final stages in particle release has recently been proposed and a cellular protein that appears to bind directly to the Gag precursor has been identified. Each of these observations helps to clarify previously obscure aspects of viral replication and points towards potential targets for the design of novel therapies.
当HIV-1病毒从宿主细胞表面出芽时,其核心颗粒在宿主细胞膜上组装。构成核心的结构蛋白和酶作为两种多蛋白前体Gag和GagPol的一部分进行翻译。Gag前体包含核心的结构蛋白,对于指导颗粒组装和出芽既是必需的也是充分的。在过去几年中,我们对驱动颗粒组装的相互作用的理解取得了重大进展。具体而言,已鉴定并部分表征了Gag前体中指导膜结合、Gag-Gag相互作用和颗粒出芽的决定因素。也描述了有利于颗粒组装和出芽的宿主细胞膜亚结构域。最后,最近有人提出细胞过程在介导颗粒释放的最后阶段中可能发挥的作用,并且已鉴定出一种似乎直接与Gag前体结合的细胞蛋白。这些观察结果中的每一个都有助于阐明病毒复制以前模糊不清的方面,并指出新型疗法设计的潜在靶点。