An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-02

AUTHORS

Marit J. van Gils, Tom L. G. M. van den Kerkhof, Gabriel Ozorowski, Christopher A. Cottrell, Devin Sok, Matthias Pauthner, Jesper Pallesen, Natalia de Val, Anila Yasmeen, Steven W. de Taeye, Anna Schorcht, Stephanie Gumbs, Inez Johanna, Karen Saye-Francisco, Chi-Hui Liang, Elise Landais, Xiaoyan Nie, Laura K. Pritchard, Max Crispin, Garnett Kelsoe, Ian A. Wilson, Hanneke Schuitemaker, Per Johan Klasse, John P. Moore, Dennis R. Burton, Andrew B. Ward, Rogier W. Sanders

ABSTRACT

The induction by vaccination of broadly neutralizing antibodies (bNAbs) capable of neutralizing various HIV-1 viral strains is challenging, but understanding how a subset of HIV-infected individuals develops bNAbs may guide immunization strategies. Here, we describe the isolation and characterization of the bNAb ACS202 from an elite neutralizer that recognizes a new, trimer-specific and cleavage-dependent epitope at the gp120-gp41 interface of the envelope glycoprotein (Env), involving the glycan N88 and the gp41 fusion peptide. In addition, an Env trimer, AMC011 SOSIP.v4.2, based on early virus isolates from the same elite neutralizer, was constructed, and its structure by cryo-electron microscopy at 6.2 Å resolution reveals a closed, pre-fusion conformation similar to that of the BG505 SOSIP.664 trimer. The availability of a native-like Env trimer and a bNAb from the same elite neutralizer provides the opportunity to design vaccination strategies aimed at generating similar bNAbs against a key functional site on HIV-1. More... »

PAGES

nmicrobiol2016199

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nmicrobiol.2016.199

DOI

http://dx.doi.org/10.1038/nmicrobiol.2016.199

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1046144185

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27841852


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