Envelope glycoprotein gp160 (HIV-1) (gp160)

Envelope glycoprotein gp160 of HIV-1 is the polyprotein precursor that forms the viral envelope glycoprotein complex. Synthesized as gp160, it oligomerizes into trimers and undergoes glycosylation in the endoplasmic reticulum and Golgi apparatus. Proteolytic cleavage by host furin or furin-like proteases yields two functional subunits: surface glycoprotein gp120, which binds to the host CD4 receptor and a co-receptor (usually CCR5 or CXCR4), and transmembrane glycoprotein gp41, which mediates fusion of the viral and host cell membranes. This entry step is essential for HIV infection, and both natural (neutralizing antibodies) and therapeutic (fusion/entry inhibitors) interventions target components of this process. Extreme conformational flexibility, heavy glycosylation, and structural heterogeneity allow gp160 to evade host immune responses and complicate vaccine development. Gp160 and its cleavage products are central to viral infectivity, transmission, and immune recognition[1][3][4][6][7][8][10].

Other names

HIV-1 gp160Env precursorHIV-1 envelope glycoprotein precursorEnv polyproteinHIV-1 Env

Inhibition of gp41-mediated membrane fusion; Blockade of CD4 or co-receptor (CCR5/CXCR4) interaction by gp120