外域
疱疹病毒糖蛋白B
糖蛋白
脂质双层融合
单纯疱疹病毒
水泡性口炎病毒
病毒学
生物
化学
病毒进入
病毒
分子生物学
受体
生物化学
病毒复制
作者
Ekaterina E. Heldwein,Huan Lou,Florent C. Bender,Gary H. Cohen,Roselyn J. Eisenberg,Stephen C. Harrison
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2006-07-14
卷期号:313 (5784): 217-220
被引量:513
标识
DOI:10.1126/science.1126548
摘要
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 α-helical coiled-coil core relates gB to class I viral membrane fusion glycoproteins; two extended β 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.
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