HIV-1 envelope glycoprotein gp160 (Env)

The HIV-1 envelope glycoprotein (Env) is a trimeric complex synthesized as a gp160 precursor and subsequently cleaved by host cell proteases into two non-covalently associated subunits: the surface glycoprotein gp120 and the transmembrane glycoprotein gp41 [2.2.1, 2.4.1]. As the sole viral protein exposed on the surface of the HIV-1 virion, Env is essential for the initiation of infection by mediating viral attachment and entry into host cells [2.4.3]. The gp120 subunit facilitates initial binding to the primary CD4 receptor and a chemokine coreceptor (typically CCR5 or CXCR4), while the gp41 subunit undergoes conformational changes to drive the fusion of the viral and host cell membranes [2.3.2, 3.1.5]. Due to its critical role in the viral life cycle, Env is a major target for antiretroviral therapies, such as attachment inhibitors and fusion inhibitors, as well as for vaccine development [2.3.1, 3.2.1]. However, the target's high genetic variability, extensive glycosylation (the "glycan shield"), and conformational flexibility present significant challenges for drug design and immune recognition [2.3.1, 2.4.2].

Other names

gp160gp120gp41Env polyproteinSurface protein gp120Transmembrane protein gp41SUTM

Attachment inhibition (gp120) and fusion inhibition (gp41) [2.1.2, 3.2.1]