Glycan Microheterogeneity at the PGT135 Antibody Recognition Site on HIV-1 gp120 Reveals a Molecular Mechanism for Neutralization Resistance.

Abstract:

:Broadly neutralizing antibodies have been isolated that bind the glycan shield of the HIV-1 envelope spike. One such antibody, PGT135, contacts the intrinsic mannose patch of gp120 at the Asn332, Asn392, and Asn386 glycosylation sites. Here, site-specific glycosylation analysis of recombinant gp120 revealed glycan microheterogeneity sufficient to explain the existence of a minor population of virions resistant to PGT135 neutralization. Target microheterogeneity and antibody glycan specificity are therefore important parameters in HIV-1 vaccine design.

journal_name

J Virol

journal_title

Journal of virology

authors

Pritchard LK,Spencer DI,Royle L,Vasiljevic S,Krumm SA,Doores KJ,Crispin M

doi

10.1128/JVI.00230-15

subject

Has Abstract

pub_date

2015-07-01 00:00:00

pages

6952-9

issue

13

eissn

0022-538X

issn

1098-5514

pii

JVI.00230-15

journal_volume

89

pub_type

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