Different receptors binding to distinct interfaces on herpes simplex virus gD can trigger events leading to cell fusion and viral entry
Different receptors binding to distinct interfaces on herpes simplex virus gD can trigger events leading to cell fusion and viral entry
复制标题
DOI：
10.1016/j.virol.2005.09.016
复制
发表时间：
2006-01-05
期刊：
影响因子：
3.7
通讯作者：
Myscofski, D
中科院分区：
文献类型：
--
作者：
Spear, PG;Manoj, S;Myscofski, D
单纯疱疹病毒包膜糖蛋白之一，称为gD，是病毒进入细胞识别的主要决定因素。其他病毒糖蛋白gB、gH和gL与gD合作介导病毒进入和细胞融合所需的膜融合。膜融合是由gD与其受体之一结合触发的。这些受体属于三种不同类型的细胞表面分子。本文综述了gD的结构和功能的最新研究结果。结果表明，gD可能承担一个以上的构象，一个在没有受体，另一个当gD结合到疱疹病毒进入介质，TNF受体家族的成员，和第三个当gD结合到nectin-1，在免疫球蛋白超家族中的细胞粘附分子。最后，信息和想法提出了关于膜融合所需的gD的近膜区域，但不是受体结合，并可能有一个角色，在激活gB，gH和gL的融合活性。(c)2005年爱思唯尔公司All rights reserved.
One of the herpes simplex virus envelope glycoproteins, designated gD, is the principal determinant of cell recognition for viral entry. Other viral glycoproteins, gB, gH and gL, cooperate with gD to mediate the membrane fusion that is required for viral entry and cell fusion. Membrane fusion is triggered by the binding of gD to one of its receptors. These receptors belong to three different classes of cell surface molecules. This review summarizes recent findings on the structure and function of gD. The results presented indicate that gD may assume more than one conformation, one in the absence of receptor, another when gD is bound to the herpesvirus entry mediator, a member of the TNF receptor family, and a third when gD is bound to nectin-1, a cell adhesion molecule in the immunoglobulin superfamily. Finally, information and ideas are presented about a membrane-proximal region of gD that is required for membrane fusion, but not for receptor binding, and that may have a role in activating the fusogenic activity of gB, gH and gL. (c) 2005 Elsevier Inc. All rights reserved.