Differential recognition of epitopes present on monomeric and oligomeric forms of gp160 glycoprotein of human immunodeficiency virus type 1 by human monoclonal antibodies

被引：16

作者：

Zeder-Lutz, G ^{[1
]}

Hoebeke, J ^{[1
]}

Van Regenmortel, MHV ^{[1
]}

机构：

[1] Inst Biol Mol & Cellulaire, CNRS, UPR 9021, F-67084 Strasbourg, France

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 2001年 / 268卷 / 10期

关键词：

HIV; antibody-antigen interaction; kinetics; surface plasmon resonance;

D O I：

10.1046/j.1432-1327.2001.02167.x

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 mechanism of infectivity neutralization of human immunodeficiency virus type 1 (HIV-1) by Ig is poorly understood. Three human monoclonal antibodies (mAbs 1b12, 2G12 and 2F5) that are able to neutralize primary isolates of HIV-1 in vitro have been shown to act synergistically. In the present study this synergy was analyzed by measuring the epitope accessibility and binding kinetics for these three mAbs with respect to monomeric and oligomeric env protein gp160 IIIB using surface plasmon resonance. The results indicate that oligomerization of gp160 affects the accessibility of some of the epitopes recognized by the mAbs and provide some insight into the mechanism of synergy between different anti-(HIV-1) mAbs.

引用

页码：2856 / 2866

页数：11

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