Crystal structure of a non-neutralizing antibody to the HIV-1 gp41 membrane-proximal external region

被引：38

作者：

Nicely, Nathan I. ^{[1
]}

Dennison, S. Moses ^{[1
]}

Spicer, Leonard ^{[2
,3
]}

Scearce, Richard M. ^{[1
]}

Kelsoe, Garnett ^{[1
,4
]}

Ueda, Yoshihiro ^{[1
,4
]}

Chen, Haiyan ^{[1
]}

Liao, Hua-Xin ^{[1
]}

Alam, S. Munir ^{[1
]}

Haynes, Barton F. ^{[1
]}

机构：

[1] Duke Univ, Sch Med, Duke Human Vaccine Inst, Durham, NC 27706 USA

[2] Duke Univ, Dept Biochem, Durham, NC USA

[3] Duke Univ, Dept Radiol, Durham, NC 27710 USA

[4] Duke Univ, Dept Immunol, Durham, NC USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2010年 / 17卷 / 12期

关键词：

IMMUNODEFICIENCY-VIRUS TYPE-1; BROADLY NEUTRALIZING ANTIBODIES; HUMAN MONOCLONAL-ANTIBODIES; 2F5; BINDING; EPITOPE; FUSION; COMPLEMENTARITY; RECOGNITION; 4E10;

D O I：

10.1038/nsmb.1944

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 monoclonal antibody 13H11 shares part of its epitope in the HIV-1 gp41 membrane-proximal external region (MPER) with the rare, broadly neutralizing human antibody 2F5. Although 13H11 partially cross-blocked 2F5 binding, 13H11 is non-neutralizing and does not block 2F5 neutralization. We show that unlike 2F5, 13H11 binds to a well-defined helical MPER structure that is consistent with the structure of gp41 in a post-fusion six-helix bundle conformation.

引用

页码：1492 / 1494

页数：3

共 21 条

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