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Crystal Structure of a Neutralizing Human IgG Against HIV-1: A Template for Vaccine Design

Science  10 Aug 2001:
Vol. 293, Issue 5532, pp. 1155-1159
DOI: 10.1126/science.1061692

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Abstract

We present the crystal structure at 2.7 angstrom resolution of the human antibody IgG1 b12. Antibody b12 recognizes the CD4-binding site of human immunodeficiency virus–1 (HIV-1) gp120 and is one of only two known antibodies against gp120 capable of broad and potent neutralization of primary HIV-1 isolates. A key feature of the antibody-combining site is the protruding, finger-like long CDR H3 that can penetrate the recessed CD4-binding site of gp120. A docking model of b12 and gp120 reveals severe structural constraints that explain the extraordinary challenge in eliciting effective neutralizing antibodies similar to b12. The structure, together with mutagenesis studies, provides a rationale for the extensive cross-reactivity of b12 and a valuable framework for the design of HIV-1 vaccines capable of eliciting b12-like activity.

  • * To whom correspondence should be addressed. E-mail: wilson{at}scripps.edu, burton{at}scripps.edu

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