Neutralizing ebolavirus: structural insights into the envelope glycoprotein and antibodies targeted against it

被引：55

作者：

Lee, Jeffrey E. ^{[1
]}

Saphire, Erica Ollmann ^{[1
,2
]}

机构：

[1] Scripps Res Inst, Dept Immunol & Microbial Sci, La Jolla, CA 92037 USA

[2] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2009年 / 19卷 / 04期

基金：

加拿大健康研究院; 美国国家卫生研究院;

关键词：

VIRAL MEMBRANE-FUSION; VIRUS GLYCOPROTEIN; HEMORRHAGIC-FEVER; MONOCLONAL-ANTIBODIES; VIRION GLYCOPROTEINS; CRYSTAL-STRUCTURE; INFLUENZA-VIRUS; CELLULAR ENTRY; INFECTION; BINDING;

D O I：

10.1016/j.sbi.2009.05.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 GIP 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.

引用

页码：408 / 417

页数：10

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