Completeness of HIV-1 Envelope Glycan Shield at Transmission Determines Neutralization Breadth.

ABSTRACT: Densely arranged N-linked glycans shield the HIV-1 envelope (Env) trimer from antibody recognition. Strain-specific breaches in this shield (glycan holes) can be targets of vaccine-induced neutralizing antibodies that lack breadth. To understand the interplay between glycan holes and neutralization breadth in HIV-1 infection, we developed a sequence- and structure-based approach to identify glycan holes for individual Env sequences that are shielded in most M-group viruses. Applying this approach to 12 longitudinally followed individuals, we found that transmitted viruses with more intact glycan shields correlated with development of greater neutralization breadth. Within 2 years, glycan acquisition filled most glycan holes present at transmission, indicating escape from hole-targeting neu

SUBMITTER: Wagh K 

PROVIDER: S-EPMC6426304 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature