Herpes simplex virus glycoprotein D bound to the human receptor HveA
Herpes simplex virus glycoprotein D bound to the human receptor HveA
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DOI：
10.1016/s1097-2765(01)00298-2
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发表时间：
2001-07-01
期刊：
影响因子：
16
通讯作者：
Wiley, DC
中科院分区：
文献类型：
--
作者：
Carfí, A;Willis, SH;Wiley, DC
单纯疱疹病毒（HSV）感染需要病毒包膜糖蛋白D（gD）与细胞表面受体结合。我们报道了一种可溶性的、截短的gD胞外域单独存在以及与它的细胞受体HveA的胞外域形成复合物时的X射线结构。两个结合的阴离子提示了另一种gD受体——一种3 - O - 磺化硫酸乙酰肝素可能的结合位点。出乎意料的是，这些结构揭示了在gD核心处有一种类似V型的免疫球蛋白（Ig）折叠，它与细胞黏附分子密切相关，并且两侧有较大的N端和C端延伸。gD的受体结合区段，即一个N端发夹结构，似乎在构象上具有灵活性，这表明伴随结合发生的构象变化可能是病毒进入机制的一部分。
Herpes simplex virus (HSV) infection requires binding of the viral envelope glycoprotein D (gD) to cell surface receptors. We report the X-ray structures of a soluble, truncated ectodomain of go both alone and in complex with the ectodomain of its cellular receptor HveA. Two bound anions suggest possible binding sites for another go receptor, a 3-O-sulfonated heparan sulfate. Unexpectedly, the structures reveal a V-like immunoglobulin tig) fold at the core of go that is closely related to cellular adhesion molecules and flanked by large N- and C-terminal extensions. The receptor binding segment of gD, an N-terminal hairpin, appears conformationally flexible, suggesting that a conformational change accompanying binding might be part of the viral entry mechanism.