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Van Ryk, Donald; Wyatt, Richard; Dey, Barna; Zhang, Mei-Yun; Nabel, Gary J; Xu, Ling; Xiang, Shi-Hua; Dimitrov, Dimiter S; Sodroski, Joseph; Arthos, James; Yang, Xinzhen; Zhou, Tongqing; Kwong, Peter D; Hessell, Ann J; Burton, Dennis R; Zwick, Michael B
Nature, 02/2007, Letnik: 445, Številka: 7129Journal Article
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.
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