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The HIV-1 envelope glycoprotein trimer is covered by an array of N-linked glycans that shield it from immune surveillance. The high density of glycans on the trimer surface imposes steric constraints limiting the actions of glycan-processing enzymes, so that multiple under-processed structures remain on specific areas. These oligomannose glycans are recognized by broadly neutralizing antibodies (bNAbs) that are not thwarted by the glycan shield but, paradoxically, target it. Our site-specific glycosylation analysis of a soluble, recombinant trimer (BG505 SOSIP.664) maps the extremes of simplicity and diversity of glycan processing at individual sites and reveals a mosaic of dense clusters of oligomannose glycans on the outer domain. Although individual sites usually minimally affect the global integrity of the glycan shield, we identify examples of how deleting some glycans can subtly influence neutralization by bNAbs that bind at distant sites. The network of bNAb-targeted glycans should be preserved on vaccine antigens.

Original publication

DOI

10.1016/j.celrep.2016.02.058

Type

Journal article

Journal

Cell Rep

Publication Date

22/03/2016

Volume

14

Pages

2695 - 2706

Keywords

Antibodies, Neutralizing, Chromatography, Affinity, Chromatography, High Pressure Liquid, Glycopeptides, Glycosylation, HEK293 Cells, HIV Envelope Protein gp120, HIV-1, Humans, Polysaccharides, Recombinant Proteins, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization