HIV-1 envelope glycoprotein gp160 (gp160) (gp160)

The HIV-1 envelope glycoprotein gp160 is the primary viral protein responsible for mediating entry into host CD4+ T-cells (UniProt: P04578). It is synthesized as a precursor that is subsequently cleaved by host cell proteases into two non-covalently associated subunits: the surface subunit gp120 and the transmembrane subunit gp41 (PubMed: 11544310). gp120 facilitates initial attachment by binding to the host CD4 receptor and a coreceptor, typically CCR5 or CXCR4, while gp41 undergoes a dramatic conformational change to drive the fusion of viral and cellular membranes (NIH: NIAID HIV/AIDS). As the only viral protein exposed on the surface of the virion, gp160 is a critical target for both the host immune response and therapeutic intervention. Drugs targeting this protein include attachment inhibitors like fostemsavir, which binds gp120, and fusion inhibitors like enfuvirtide, which targets gp41 (FDA: Rukobia Label; FDA: Fuzeon Label). However, the high mutation rate of the HIV-1 genome and the presence of an extensive glycan shield present significant challenges for vaccine development and long-term drug efficacy (PubMed: 29133882).

Other names

Envgp120/gp41 complexEnvelope surface glycoprotein gp120Transmembrane glycoprotein gp41HIV-1 Env

Inhibition of viral entry by blocking gp120 attachment to CD4 receptors or preventing gp41-mediated membrane fusion (PubMed: 32663444, FDA: Rukobia Label).