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Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design.

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Affiliations

  • 1. Department of Molecular Biology, Department of Immunology, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
      Authors
    • Saphire EO 1
    (1 author)

ORCIDs linked to this article

Science, 01 Aug 2001, 293(5532):1155-1159
https://doi.org/10.1126/science.1061692 PMID: 11498595 

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.

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Read article at publisher's site: https://doi.org/10.1126/science.1061692

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Funding 

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NIAID NIH HHS (2)

NIGMS NIH HHS (1)