Lee Jeffrey E, Saphire Erica Ollmann
Department of Immunology & Microbial Science, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA, Tel.: +1 858 784 7976.
Future Virol. 2009;4(6):621-635. doi: 10.2217/fvl.09.56.
Ebolavirus (EBOV) is a highly virulent pathogen capable of causing a severe hemorrhagic fever with 50-90% lethality. The EBOV glycoprotein (GP) is the only virally expressed protein on the virion surface and is critical for attachment to host cells and catalysis of membrane fusion. Hence, the EBOV GP is a critical component of vaccines as well as a target of neutralizing antibodies and inhibitors of attachment and fusion. The crystal structure of the Zaire ebolavirus GP in its trimeric, prefusion conformation (3 GP(1) plus 3 GP(2)) in complex with a neutralizing antibody fragment, derived from a human survivor of the 1995 Kikwit outbreak, was recently determined. This is the first near-complete structure of any filovirus glycoprotein. The overall molecular architecture of the Zaire ebolavirus GP and its role in viral entry and membrane fusion are discussed in this article.
埃博拉病毒(EBOV)是一种高致病性病原体,能够引发严重的出血热,致死率达50%-90%。埃博拉病毒糖蛋白(GP)是病毒粒子表面唯一由病毒表达的蛋白质,对于病毒附着于宿主细胞以及催化膜融合至关重要。因此,埃博拉病毒GP是疫苗的关键成分,也是中和抗体以及附着和融合抑制剂的作用靶点。最近确定了扎伊尔埃博拉病毒GP三聚体、前融合构象(3个GP(1)加上3个GP(2))与一个中和抗体片段的晶体结构,该抗体片段源自1995年基奎特疫情的一名人类幸存者。这是首个接近完整的丝状病毒糖蛋白结构。本文将讨论扎伊尔埃博拉病毒GP的整体分子结构及其在病毒进入和膜融合中的作用。