Shaw Pamela L, Kirschner Austin N, Jardetzky Theodore S, Longnecker Richard
Department of Microbiology and Immunology, The Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
Virus Genes. 2010 Jun;40(3):307-19. doi: 10.1007/s11262-010-0455-x. Epub 2010 Feb 17.
Epstein-Barr virus (EBV) glycoprotein 42 (gp42) is a membrane protein essential for fusion and entry of EBV into host B-lymphocytes. Gp42 is a member of the protein-fold family C-type lectin or lectin-like domains (CLECT or CTLD) and specifically is classified as a natural-killer receptor (NKR)-like CLECT. Literature review and phylogenetic comparison show that EBV gp42 shares a common structure with other NKR-like CLECTs and possibly with many viral CTLDs, but does not appear to exhibit some common binding characteristics of many CTLDs, such as features required for calcium binding. The flexible N-terminal region adjacent to the CTLD fold is important for binding to other EBV glycoproteins and for a cleavage site that is necessary for infection of host cells. From structural studies of gp42 unbound and bound to receptor and extensive mutational analysis, a general model of how gp42 triggers membrane fusion utilizing both the flexible N-terminal region and the CTLD domain has emerged.
爱泼斯坦-巴尔病毒（EBV）糖蛋白42（gp42）是一种膜蛋白，对于EBV融合并进入宿主B淋巴细胞至关重要。Gp42是蛋白折叠家族C型凝集素或凝集素样结构域（CLECT或CTLD）的成员，具体归类为自然杀伤受体（NKR）样CLECT。文献综述和系统发育比较表明，EBV gp42与其他NKR样CLECT以及可能与许多病毒CTLD具有共同结构，但似乎不具备许多CTLD的一些常见结合特征，例如钙结合所需的特征。与CTLD折叠相邻的灵活N端区域对于与其他EBV糖蛋白结合以及对于宿主细胞感染所必需的切割位点很重要。通过对未结合和结合受体的gp42的结构研究以及广泛的突变分析，已经出现了一个关于gp42如何利用灵活的N端区域和CTLD结构域触发膜融合的通用模型。
