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This article is part of the supplement: AIDS Vaccine 2009

Open Access Oral presentation

S021-05 OA. Broadly neutralizing anti-HIV-1 antibodies disrupt a hinge-related function of gp41 at the membrane interface

L Song1, ZJ Sun2, KE Coleman1, MB Zwick3, JS Gach3, J Wang2, EL Reinherz1, G Wagner2 and M Kim1*

  • * Corresponding author: M Kim

Author Affiliations

1 Cancer Vaccine Center, Dana-Farber Cancer Institute, Boston, MA, USA

2 Harvard Medical School, Boston, MA, USA

3 The Scripps Research Institute, La Jolla, CA, USA

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Retrovirology 2009, 6(Suppl 3):O5 doi:10.1186/1742-4690-6-S3-O5

Published: 22 October 2009

First paragraph (this article has no abstract)

A vaccine capable of stimulating protective anti-viral antibody responses is needed to curtail the global Acquired Immunodeficiency Syndrome (AIDS) epidemic caused by HIV-1. Although rarely elicited during the course of natural infection or upon conventional vaccination, the membrane proximal ectodomain region (MPER) of the HIV-1 gp41 envelope protein subunit is the target of three such human broadly neutralizing antibodies (BNAbs): 4E10, 2F5 and Z13e1. How these BNAbs bind to their lipid-embedded epitopes and mediate anti-viral activity are unclear, but such information might offer important insight into a world-wide health imperative.