单纯疱疹病毒1型糖蛋白B的晶体结构

Crystal structure of glycoprotein B from herpes simplex virus 1.

作者信息

Heldwein Ekaterina E, Lou Huan, Bender Florent C, Cohen Gary H, Eisenberg Roselyn J, Harrison Stephen C

机构信息

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 320 Longwood Avenue, Boston, MA 02115, USA.

出版信息

Science. 2006 Jul 14;313(5784):217-20. doi: 10.1126/science.1126548.

DOI:10.1126/science.1126548

PMID:16840698

Abstract

Glycoprotein B (gB) is the most conserved component of the complex cell-entry machinery of herpes viruses. A crystal structure of the gB ectodomain from herpes simplex virus type 1 reveals a multidomain trimer with unexpected homology to glycoprotein G from vesicular stomatitis virus (VSV G). An alpha-helical coiled-coil core relates gB to class I viral membrane fusion glycoproteins; two extended beta hairpins with hydrophobic tips, homologous to fusion peptides in VSV G, relate gB to class II fusion proteins. Members of both classes accomplish fusion through a large-scale conformational change, triggered by a signal from a receptor-binding component. The domain connectivity within a gB monomer would permit such a rearrangement, including long-range translocations linked to viral and cellular membranes.

摘要

糖蛋白B（gB）是疱疹病毒复杂细胞进入机制中最保守的成分。1型单纯疱疹病毒gB胞外域的晶体结构揭示了一种多结构域三聚体，与水疱性口炎病毒（VSV G）的糖蛋白G具有意想不到的同源性。一个α螺旋卷曲螺旋核心将gB与I类病毒膜融合糖蛋白联系起来；两个带有疏水末端的延伸β发夹，与VSV G中的融合肽同源，将gB与II类融合蛋白联系起来。这两类成员都通过受体结合成分发出的信号触发的大规模构象变化来完成融合。gB单体中的结构域连接性将允许这种重排，包括与病毒和细胞膜相关的长距离易位。