Human immunodeficiency virus type 1 envelope glycoprotein gp160 precursor (gp160)

Human immunodeficiency virus type 1 envelope glycoprotein gp160 precursor (gp160) is a nonfusogenic polyprotein synthesized by HIV-1 within host cells. After glycosylation and oligomerization into trimers in the endoplasmic reticulum, gp160 is cleaved by host furin protease in the Golgi apparatus to produce two subunits: the surface glycoprotein gp120 and the transmembrane glycoprotein gp41. These subunits assemble as non-covalently linked heterodimers, with three such dimers forming functional viral spikes on the HIV surface. gp120 binds to the host CD4 receptor and a coreceptor (CCR5 or CXCR4) to initiate viral entry, while gp41 facilitates fusion of viral and host cell membranes. gp160 (and its subunits) is the key molecular target for anti-HIV therapies, especially fusion inhibitors, entry inhibitors, and neutralizing antibodies. The protein is heavily glycosylated and highly variable, which enables immune evasion and represents a major barrier for vaccine and drug development.

Other names

Envelope glycoprotein gp160HIV-1 EnvHIV-1 envelope glycoprotein precursorSU-TM polyprotein precursorgp120-gp41 precursor

Drugs and antibodies may block CD4 binding (preventing initial attachment with host cell) Prevent conformational changes needed for membrane fusion Interfere with gp41-mediated fusion mechanism Neutralize viral particles by binding exposed conserved epitopes and blocking infectivity