Envelope glycoprotein trimer of HIV-1 (HIV-1 Env trimer)

The **Envelope glycoprotein trimer of HIV-1** (commonly called "HIV-1 Env trimer") is a membrane-anchored homotrimeric complex composed of three gp120 and three gp41 subunits, derived from cleavage of the gp160 precursor[4][5][3]. Located on the surface of HIV-1 virions, the Env trimer mediates viral entry by first binding to the CD4 receptor and a co-receptor (CCR5 or CXCR4) on host cells, triggering conformational changes that drive the gp41-mediated fusion of the viral and host membranes[1][2][3][5]. Env is the only HIV-1 structure exposed to the host immune system and is the main target for neutralizing antibodies; its extreme sequence variability, extensive glycosylation, and conformational flexibility help the virus evade immune responses[3][6]. Because of these properties, the Env trimer is a major focus for vaccine and therapeutic development, as well as basic research into viral entry and immune evasion mechanisms[3][6][1].

Other names

HIV-1 Env trimerHIV-1 envelope glycoproteingp160 trimergp120-gp41 trimerHIV-1 envelope spike

Inhibition of viral membrane fusion; Blockade of CD4 or co-receptor binding