Roles of Virion-Incorporated CD162 (PSGL-1), CD43, and CD44 in HIV-1 Infection of T Cells

Abstract

Nascent HIV-1 particles incorporate the viral envelope glycoprotein and multiple host transmembrane proteins during assembly at the plasma membrane. At least some of these host transmembrane proteins on the surface of virions are reported as pro-viral factors that enhance virus attachment to target cells or facilitate trans-infection of CD4+ T cells via interactions with non-T cells. In addition to the pro-viral factors, anti-viral transmembrane proteins are incorporated into progeny virions. These virion-incorporated transmembrane proteins inhibit HIV-1 entry at the point of attachment and fusion. In infected polarized CD4+ T cells, HIV-1 Gag localizes to a rear-end protrusion known as the uropod. Regardless of cell polarization, Gag colocalizes with and promotes the virion incorporation of a subset of uropod-directed host transmembrane proteins, including CD162, CD43, and CD44. Until recently, the functions of these virion-incorporated proteins had not been clear. Here, we review the recent findings about the roles played by virion-incorporated CD162, CD43, and CD44 in HIV-1 spread to CD4+ T cells.

HIV-1 interaction with an O-glycan-specific bacterial lectin enhances virus infectivity and resistance to neutralization by antibodies

“…Polymers such as polybrene and DEAE Dextran that are commonly used to facilitate HIV-1 infection and lentivirus transduction also enhance virus-cell binding through a similar mechanism 65 . Apart from viral Env, O-glycan-bearing cell membrane proteins such as CD162 (P-selectin glycoprotein ligand-1), CD43 (sialophorin), and CD44 (E-selectin ligand), are present on the surfaces of HIV-1 virions [66][67][68] . Nonetheless, the extent to which SLBR-N and similar lectins bind to O-glycans on cellular proteins relative to Env is yet unknown.…”