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

TitleGlycan Microheterogeneity at the PGT135 Antibody Recognition Site on HIV-1 gp120 Reveals a Molecular Mechanism for Neutralization Resistance.
Publication TypeJournal Article
Year of Publication2015
AuthorsPritchard LK, Spencer DIR, Royle L, Vasiljevic S, Krumm SA, Doores KJ, Crispin M
JournalJ Virol
Volume89
Issue13
Pagination6952-9
Date Published07/01/2015
ISSN1098-5514
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.

DOI10.1128/JVI.00230-15
Alternate JournalJ. Virol.
PubMed ID25878100
PubMed Central IDPMC4468474
Grant List1UM1AI100663 / AI / NIAID NIH HHS / United States
MR/K024426/1 / / Medical Research Council / United Kingdom
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