Lee Jeffrey E, Saphire Erica Ollmann
Department of Immunology and Microbial Science, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Curr Opin Struct Biol. 2009 Aug;19(4):408-17. doi: 10.1016/j.sbi.2009.05.004. Epub 2009 Jun 24.
The ebolavirus (EBOV) envelope glycoprotein (GP) is solely responsible for viral attachment to, fusion with, and entry of new host cells, and consequently is a major target of vaccine design efforts. Recently determined crystal structures of key antibodies in complex with their EBOV epitopes have provided insights into the molecular architecture of GP and defined likely hotspots for viral neutralization. In this review, we discuss the structural basis for antibody-mediated neutralization of ebolavirus and its implications for novel therapeutic or vaccine strategies.
埃博拉病毒（EBOV）包膜糖蛋白（GP）单独负责病毒与新宿主细胞的附着、融合及进入，因此是疫苗设计工作的主要靶点。最近确定的与EBOV表位结合的关键抗体的晶体结构，为GP的分子结构提供了见解，并确定了可能的病毒中和热点。在本综述中，我们讨论了抗体介导的埃博拉病毒中和作用的结构基础及其对新型治疗或疫苗策略的影响。
