Broadly Neutralizing HIV Antibodies Define a Glycan-Dependent Epitope on the Prefusion Conformation of gp41 on Cleaved Envelope Trimers.

TitleBroadly Neutralizing HIV Antibodies Define a Glycan-Dependent Epitope on the Prefusion Conformation of gp41 on Cleaved Envelope Trimers.
Publication TypeJournal Article
Year of Publication2014
AuthorsFalkowska E, Le KM, Ramos A, Doores KJ, Lee J H, Blattner C, Ramirez A, Derking R, van Gils MJ, Liang C-H, McBride R, von Bredow B, Shivatare SS, Wu C-Y, Chan-Hui P-Y, Liu Y, Feizi T, Zwick MB, Koff WC, Seaman MS, Swiderek K, Moore JP, Evans D, Paulson JC, Wong C-H, Ward AB, Wilson IA, Sanders RW, Poignard P, Burton DR
JournalImmunity
Volume40
Issue5
Start Page657
Pagination657-68
Date Published05/15/2014
ISSN1097-4180
Abstract

Broadly neutralizing HIV antibodies are much sought after (a) to guide vaccine design, both as templates and as indicators of the authenticity of vaccine candidates, (b) to assist in structural studies, and (c) to serve as potential therapeutics. However, the number of targets on the viral envelope spike for such antibodies has been limited. Here, we describe a set of human monoclonal antibodies that define what is, to the best of our knowledge, a previously undefined target on HIV Env. The antibodies recognize a glycan-dependent epitope on the prefusion conformation of gp41 and unambiguously distinguish cleaved from uncleaved Env trimers, an important property given increasing evidence that cleavage is required for vaccine candidates that seek to mimic the functional HIV envelope spike. The availability of this set of antibodies expands the number of vaccine targets on HIV and provides reagents to characterize the native envelope spike.

DOI10.1016/j.immuni.2014.04.009
Alternate JournalImmunity
PubMed ID24768347
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