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TitleAn HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability.
Journal, issue, pagesNat Microbiol, Vol. 2, Page 16199, Year 2016
Publish dateNov 14, 2016
AuthorsMarit 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 /
PubMed AbstractThe 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 ...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.
External linksNat Microbiol / PubMed:27841852 / PubMed Central
MethodsEM (single particle)
Resolution6.2 - 21.0 Å
Structure data

EMDB-8299:
AMC011 HIV-1 Env SOSIP trimer in complex with autologous anti-HIV antibody ACS202
Method: EM (single particle) / Resolution: 21.0 Å

EMDB-8302:
HIV Clade B Env SOSIP ectodomain trimer from the Amsterdam Cohort Study patient AMC011 in complex with Fab from IgG PGV04
Method: EM (single particle) / Resolution: 6.2 Å

Source
  • Human immunodeficiency virus 1
  • Homo sapiens (human)

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