1型人类免疫缺陷病毒包膜糖蛋白三聚体在病毒进入宿主细胞过程中的亚基化学计量学
Subunit stoichiometry of human immunodeficiency virus type 1 envelope glycoprotein trimers during virus entry into host cells.
作者信息
Yang Xinzhen, Kurteva Svetla, Ren Xinping, Lee Sandra, Sodroski Joseph
机构信息
Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Harvard Medical School, 44 Binney Street, JFB 824, Boston, Massachusetts 02115, USA.
出版信息
J Virol. 2006 May;80(9):4388-95. doi: 10.1128/JVI.80.9.4388-4395.2006.
Abstract
The envelope glycoproteins of human immunodeficiency virus type 1 (HIV-1) function as a homotrimer of gp120/gp41 heterodimers to support virus entry. During the process of virus entry, an individual HIV-1 envelope glycoprotein trimer binds the cellular receptors CD4 and CCR5/CXCR4 and mediates the fusion of the viral and the target cellular membranes. By studying the function of heterotrimers between wild-type and nonfunctional mutant envelope glycoproteins, we found that two wild-type subunits within an envelope glycoprotein trimer are required to support virus entry. Complementation between HIV-1 envelope glycoprotein mutants defective in different functions to allow virus entry was not evident. These results assist our understanding of the mechanisms whereby the HIV-1 envelope glycoproteins mediate virus entry and membrane fusion and guide attempts to inhibit these processes.
摘要
人类免疫缺陷病毒1型（HIV-1）的包膜糖蛋白作为gp120/gp41异二聚体的同源三聚体发挥作用，以支持病毒进入。在病毒进入过程中，单个HIV-1包膜糖蛋白三聚体结合细胞受体CD4和CCR5/CXCR4，并介导病毒膜与靶细胞膜的融合。通过研究野生型和无功能突变包膜糖蛋白之间的异三聚体功能，我们发现包膜糖蛋白三聚体内的两个野生型亚基是支持病毒进入所必需的。不同功能缺陷的HIV-1包膜糖蛋白突变体之间允许病毒进入的互补作用并不明显。这些结果有助于我们理解HIV-1包膜糖蛋白介导病毒进入和膜融合的机制，并指导抑制这些过程的尝试。
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