| Literature DB >> 27841852 |
Marit J van Gils1,2, Tom L G M van den Kerkhof1,3, Gabriel Ozorowski4, Christopher A Cottrell4, Devin Sok2, Matthias Pauthner2, Jesper Pallesen4, Natalia de Val4, Anila Yasmeen5, Steven W de Taeye1, Anna Schorcht1, Stephanie Gumbs1, Inez Johanna1, Karen Saye-Francisco2, Chi-Hui Liang2, Elise Landais2, Xiaoyan Nie6, Laura K Pritchard7, Max Crispin7, Garnett Kelsoe6, Ian A Wilson4, Hanneke Schuitemaker3,8, Per Johan Klasse5, John P Moore5, Dennis R Burton2,9, Andrew B Ward4, Rogier W Sanders1,5.
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.Entities:
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Year: 2016 PMID： 27841852 PMCID： PMC5372380 DOI： 10.1038/nmicrobiol.2016.199
Source DB: PubMed Journal: Nat Microbiol ISSN： 2058-5276 Impact factor: 17.745