HIV-1 Glycan Density Drives the Persistence of the Mannose Patch within an Infected Individual.

ABSTRACT: The HIV envelope glycoprotein (Env) is extensively modified with host-derived N-linked glycans. The high density of glycosylation on the viral spike limits enzymatic processing, resulting in numerous underprocessed oligomannose-type glycans. This extensive glycosylation not only shields conserved regions of the protein from the immune system but also acts as a target for anti-HIV broadly neutralizing antibodies (bnAbs). In response to the host immune system, the HIV glycan shield is constantly evolving through mutations affecting both the positions and numbers of potential N-linked glycosylation sites (PNGSs). Here, using longitudinal Env sequences from a clade C-infected individual (CAP256), we measured the impact of the shifting glycan shield during HIV infection on the abundance of olig

SUBMITTER: Coss KP 

PROVIDER: S-EPMC5126371 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature