Addition of a single gp120 glycan confers increased binding to dendritic cell-specific ICAM-3-grabbing nonintegrin and neutralization escape to human immunodeficiency virus type 1.

ABSTRACT: The potential role of dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN) binding in human immunodeficiency virus transmission across the mucosal barrier was investigated by assessing the ability of simian-human immunodeficiency chimeric viruses (SHIVs) showing varying degrees of mucosal transmissibility to bind the DC-SIGN expressed on the surface of transfected cells. We found that gp120 of the highly transmissible, pathogenic CCR5-tropic SHIV(SF162P3) bound human and rhesus DC-SIGN with an efficiency threefold or greater than that of gp120 of the nonpathogenic, poorly transmissible parental SHIV(SF162), and this increase in binding to the DC-SIGN of the SHIV(SF162P3) envelope gp120 translated into an enhancement of T-cell infection in trans. The presence of an additional glyca

SUBMITTER: Lue J 

PROVIDER: S-EPMC136558 | biostudies-literature | 2002 Oct

REPOSITORIES: biostudies-literature