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This article is part of the supplement: AIDS Vaccine 2009

Open Access Poster presentation

P19-28. The V3 region of HIV-1: from NMR to vaccine design

A Moseri2, F Naider1 and J Anglister2*

  • * Corresponding author: J Anglister

Author Affiliations

1 City University of New York, New York, USA

2 Structural Biology, Weizmann Institute of Science, Rehovot, Israel

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Retrovirology 2009, 6(Suppl 3):P348 doi:10.1186/1742-4690-6-S3-P348

Published: 22 October 2009

First paragraph (this article has no abstract)

The V3 loop is one of the few epitopes to which broadly neutralizing antibody response can be directed. The most potent and most broadly neutralizing anti-V3 antibody to date is the human monoclonal antibody 447-52D. Using NMR spectroscopy, we studied the conformation of several V3 peptides in complex with 447-52D. The flexible V3 peptides were found to adopt a β-hairpin conformation when bound to this antibody. Using disulfide bonds we constrained V3 peptides to adopt a conformation similar to those of V3 peptides bound to 447-52D.