EMD-8302

Single-particle
6.2 Å
EMD-8302 Deposition: 28/07/2016
Map released: 21/09/2016
Last modified: 14/02/2018
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-8302

HIV Clade B Env SOSIP ectodomain trimer from the Amsterdam Cohort Study patient AMC011 in complex with Fab from IgG PGV04

EMD-8302

Single-particle
6.2 Å
EMD-8302 Deposition: 28/07/2016
Map released: 21/09/2016
Last modified: 14/02/2018
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens, Human immunodeficiency virus 1
Sample: HIV Clade B Env SOSIP ectodomain trimer from the Amsterdam Cohort Study patient AMC011 in complex with Fab from IgG PGV04

Deposition Authors: Pallesen J, de Val N, Ozorowski G, Cottrell CA, Ward AB
An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability.
PUBMED: 27841852
DOI: doi:10.1038/nmicrobiol.2016.199
ISSN: 2058-5276
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.