Structural definition of a conserved neutralization epitope on HIV-1 gp120 View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2007-02

AUTHORS

Tongqing Zhou, Ling Xu, Barna Dey, Ann J. Hessell, Donald Van Ryk, Shi-Hua Xiang, Xinzhen Yang, Mei-Yun Zhang, Michael B. Zwick, James Arthos, Dennis R. Burton, Dimiter S. Dimitrov, Joseph Sodroski, Richard Wyatt, Gary J. Nabel, Peter D. Kwong

ABSTRACT

The remarkable diversity, glycosylation and conformational flexibility of the human immunodeficiency virus type 1 (HIV-1) envelope (Env), including substantial rearrangement of the gp120 glycoprotein upon binding the CD4 receptor, allow it to evade antibody-mediated neutralization. Despite this complexity, the HIV-1 Env must retain conserved determinants that mediate CD4 binding. To evaluate how these determinants might provide opportunities for antibody recognition, we created variants of gp120 stabilized in the CD4-bound state, assessed binding of CD4 and of receptor-binding-site antibodies, and determined the structure at 2.3 A resolution of the broadly neutralizing antibody b12 in complex with gp120. b12 binds to a conformationally invariant surface that overlaps a distinct subset of the CD4-binding site. This surface is involved in the metastable attachment of CD4, before the gp120 rearrangement required for stable engagement. A site of vulnerability, related to a functional requirement for efficient association with CD4, can therefore be targeted by antibody to neutralize HIV-1. More... »

PAGES

732

Journal

TITLE

Nature

ISSUE

7129

VOLUME

445

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature05580

DOI

http://dx.doi.org/10.1038/nature05580

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1021005596

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17301785


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