1型单纯疱疹病毒糖蛋白D在2.4纳米分辨率下的三维结构
Three-dimensional structure of herpes simplex virus type 1 glycoprotein D at 2.4-nanometer resolution.
作者信息
Pilling A, Rosenberg M F, Willis S H, Jäger J, Cohen G H, Eisenberg R J, Meredith D M, Holzenburg A
机构信息
Centre for Molecular Medicine, St. James's University Hospital, University of Leeds, Leeds LS9 7TF, United Kingdom.
出版信息
J Virol. 1999 Sep;73(9):7830-4. doi: 10.1128/JVI.73.9.7830-7834.1999.
Abstract
Herpes simplex virus type 1 glycoprotein D (gD) is essential for virus infectivity and is responsible for binding to cellular membrane proteins and subsequently promoting fusion between the virus envelope and the cell. No structural data are available for gD or for any other herpesvirus envelope protein. Here we present a three-dimensional model for the baculovirus-expressed truncated protein gD1(306t) based on electron microscopic data. We demonstrate that gD1(306t) appears as a homotetramer containing a pronounced pocket in the center of the molecule. Monoclonal antibody binding demonstrates that the molecule is oriented such that the pocket protrudes away from the virus envelope.
摘要
1型单纯疱疹病毒糖蛋白D（gD）对病毒感染性至关重要，负责与细胞膜蛋白结合，随后促进病毒包膜与细胞之间的融合。目前尚无gD或任何其他疱疹病毒包膜蛋白的结构数据。在此，我们基于电子显微镜数据，展示了杆状病毒表达的截短蛋白gD1(306t)的三维模型。我们证明gD1(306t)呈现为一种同四聚体，在分子中心含有一个明显的口袋状结构。单克隆抗体结合表明，该分子的取向使得口袋状结构从病毒包膜向外突出。
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