| Literature DB >> 25878100 |
Laura K Pritchard1, Daniel I R Spencer2, Louise Royle2, Snezana Vasiljevic1, Stefanie A Krumm3, Katie J Doores3, Max Crispin4.
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.Entities:
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Year: 2015 PMID: 25878100 PMCID: PMC4468474 DOI: 10.1128/JVI.00230-15
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103