Author:
Barnes Christopher O.,Schoofs Till,Gnanapragasam Priyanthi N.P.,Golijanin Jovana,Huey-Tubman Kathryn E.,Gruell Henning,Schommers Philipp,Suh-Toma Nina,Lee Yu Erica,Cetrulo Lorenzi Julio C.,Piechocka-Trocha Alicja,Scheid Johannes F.,West Anthony P.,Walker Bruce D.,Seaman Michael S.,Klein Florian,Nussenzweig Michel C.,Bjorkman Pamela J.
Abstract
AbstractThe induction of broadly neutralizing antibodies (bNAbs) is a potential strategy for a vaccine against HIV-1. However, most bNAbs exhibit features such as unusually high somatic hypermutation, including insertions and deletions, which make their induction challenging. VRC01-class bNAbs exhibit extraordinary breadth and potency, but also rank among the most highly somatically-mutated bNAbs. Here we describe a VRC01-class antibody isolated from a viremic controller, BG24, that has less than half the mutations of most other relatives of its class, while achieving comparable breadth and potency. A 3.8 Å X-ray crystal structure of a BG24-BG505 Env trimer complex revealed conserved contacts at the gp120 interface characteristic of the VRC01-class Abs, despite lacking common CDR3 sequence motifs. The existence of moderately-mutated CD4-binding site (CD4bs) bNAbs such as BG24 provides a simpler blueprint for CD4bs antibody induction by a vaccine, raising the prospect that such an induction might be feasible with a germline-targeting approach.TeaserAn anti-HIV-1 antibody with comparable neutralization breadth and potency to similarly-classed antibodies, with half as many mutations.
Publisher
Cold Spring Harbor Laboratory
Cited by
3 articles.
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