Mapping the Complete Glycoproteome of Virion-derived HIV-1 Gp120 Provides Insights into Broadly Neutralizing Antibody Binding

Overview

Journal Sci Rep

Specialty Science

Date 2016 Sep 9

PMID 27604319

Citations 56

Authors

Maria Panico

Laura Bouche

Daniel Binet

Michael-John OConnor

Dinah Rahman

Poh-Choo Pang

Kevin Canis

Simon J North

Ronald C Desrosiers

Elena Chertova

Brandon F Keele

Julian W Bess Jr

Jeffrey D Lifson

Stuart M Haslam

Anne Dell

Howard R Morris

Affiliations

Soon will be listed here.

Abstract

The surface envelope glycoprotein (SU) of Human immunodeficiency virus type 1 (HIV-1), gp120(SU) plays an essential role in virus binding to target CD4+ T-cells and is a major vaccine target. Gp120 has remarkably high levels of N-linked glycosylation and there is considerable evidence that this "glycan shield" can help protect the virus from antibody-mediated neutralization. In recent years, however, it has become clear that gp120 glycosylation can also be included in the targets of recognition by some of the most potent broadly neutralizing antibodies. Knowing the site-specific glycosylation of gp120 can facilitate the rational design of glycopeptide antigens for HIV vaccine development. While most prior studies have focused on glycan analysis of recombinant forms of gp120, here we report the first systematic glycosylation site analysis of gp120 derived from virions produced by infected T lymphoid cells and show that a single site is exclusively substituted with complex glycans. These results should help guide the design of vaccine immunogens.

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