Structure of Hepatitis C Virus Envelope Glycoprotein E2 Antigenic Site 412 to 423 in Complex with Antibody AP33

被引：76

作者：

Kong, Leopold ^{[1
]}

Giang, Erick ^{[2
]}

Nieusma, Travis ^{[1
]}

Robbins, Justin B. ^{[2
]}

Deller, Marc C. ^{[1
,4
]}

Stanfield, Robyn L. ^{[1
]}

Wilson, Ian A. ^{[1
,3
,4
]}

Law, Mansun ^{[2
]}

机构：

[1] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA

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

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

[4] Joint Ctr Struct Genom, La Jolla, CA USA

来源：

JOURNAL OF VIROLOGY | 2012年 / 86卷 / 23期

关键词：

NEUTRALIZATION; VACCINES; EPITOPE;

D O I：

10.1128/JVI.01939-12

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

We have determined the crystal structure of the broadly neutralizing antibody (bnAb) AP33, bound to a peptide corresponding to hepatitis C virus (HCV) E2 envelope glycoprotein antigenic site 412 to 423. Comparison with bnAb HCV1 bound to the same epitope reveals a different angle of approach to the antigen by bnAb AP33 and slight variation in its beta-hairpin conformation of the epitope. These structures establish two different modes of binding to E2 that antibodies adopt to neutralize diverse HCV.

引用

页码：13085 / 13088

页数：4

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