Human immunodeficiency virus type 1 envelope glycoprotein precursor (gp160)

The human immunodeficiency virus type 1 envelope glycoprotein precursor (gp160) is a heavily glycosylated viral glycoprotein synthesized as a polyprotein in the endoplasmic reticulum of virus-producing cells[1][2]. It oligomerizes into predominantly trimeric forms and undergoes extensive glycan processing in the Golgi apparatus[1][6]. Host cell proteases cleave gp160 to yield the mature surface subunit gp120 and transmembrane subunit gp41, which remain non-covalently associated as a functional trimer ('Env' complex)[2][3]. This trimer mediates viral entry by binding to the host cell receptor CD4 and coreceptors (CCR5 or CXCR4), followed by conformational changes that promote membrane fusion via the gp41 subunit[1][2][5]. Env is the sole HIV-specific target accessible to neutralizing antibodies, contributing to its role as a major vaccine and drug target. It further facilitates immune evasion via a dense "glycan shield" and rapid sequence variability[1][2]. Multiple antiviral agents—including entry inhibitors such as enfuvirtide—function by interrupting Env activity and limiting HIV infection[3].

Other names

HIV-1 gp160Env precursorHIV-1 envelope glycoproteinEnv

Entry inhibition (prevents gp41-mediated fusion), Neutralization (blocks gp120-CD4 binding or post-attachment events)