Overview
Publication
J Virol. 2015 Jul; 89(13):6952-9.
PubMed ID: 25878100
Title
Glycan microheterogeneity at the PGT135 antibody recognition site on HIV-1 gp120 reveals a molecular mechanism for neutralization resistance
Authors
Pritchard LK, Spencer DI, Royle L, Vasiljevic S, Krumm SA, Doores KJ, Crispin M
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.
With the publicly available data in the CAVD DataSpace we can Learn about studies, products, assays, antibodies, and publications, Find subjects with common characteristics, Plot assay results across studies and years of research, and Compare monoclonal antibodies and their neutralization curves. Data are also accessible via DataSpaceR, our R API.
Sign in to see full information about this publication and to download study data when available.
Related Studies
No related studies