HIV-1 envelope glycoprotein complex (gp120-gp41) (HIV-1 Env)

The HIV-1 envelope glycoprotein complex (Env), composed of the receptor-binding subunit gp120 and the membrane fusion subunit gp41, is a trimeric viral surface structure essential for mediating HIV entry into host cells[2][3][4]. Env is initially produced as a gp160 precursor, which is cleaved into gp120 and gp41 by host proteases[4]. The gp120 subunit binds host CD4 and chemokine receptors (CCR5 or CXCR4), inducing conformational changes that trigger gp41 to catalyze the fusion of viral and host cell membranes[1][2][3][4][5]. Gp41 executes membrane fusion through dramatic structural rearrangements, including formation of a six-helix bundle, allowing delivery of viral RNA into the host cell[1][2][3][5]. This process is targeted by antiviral drugs (notably fusion inhibitors such as enfuvirtide) and is the focus of vaccine and broadly neutralizing antibody development efforts[2][3][4]. The Env complex is a prototypic class I viral fusion protein and represents a central therapeutic target in HIV infection.

Other names

HIV envelope proteinHIV Envgp120-gp41HIV fusion proteinHIV-1 Env spikeEnv trimer

Inhibition of gp41 six-helix bundle formation (fusion inhibitors); Blockade of gp120-CD4 or gp120-coreceptor interaction; Neutralization by binding MPER (membrane proximal external region) of gp41 (antibodies); Disruption of conformational changes necessary for membrane fusion