Human immunodeficiency virus type 1 envelope glycoprotein gp41 (gp41) (gp41)

Human immunodeficiency virus type 1 envelope glycoprotein gp41 (gp41) is the transmembrane subunit of the HIV-1 envelope (Env) spike complex, which is essential for viral entry into host cells [1.2.1, 1.4.1]. It is produced by the proteolytic cleavage of the gp160 precursor protein by host cell furin-like proteases, remaining non-covalently associated with the surface subunit gp120 [1.4.1, 1.5.1]. Upon the binding of gp120 to the CD4 receptor and a coreceptor (CCR5 or CXCR4), gp41 undergoes a dramatic conformational change, extending its fusion peptide into the host cell membrane and subsequently collapsing into a stable six-helix bundle [1.2.2, 1.3.3]. This structural transition brings the viral and cellular membranes into close proximity, facilitating membrane fusion and the release of the viral core into the cytoplasm [1.3.1, 1.5.3]. Beyond its role in entry, gp41 has been implicated in the pathogenesis of AIDS by inducing apoptosis in uninfected bystander cells through hemifusion mechanisms [1.3.2]. As a therapeutic target, gp41 is inhibited by fusion inhibitors like enfuvirtide, which bind to the heptad repeat regions to prevent the formation of the six-helix bundle [1.3.4, 1.5.3].

Other names

Transmembrane glycoprotein gp41TMEnv gp41HIV-1 transmembrane protein gp41gp41 subunit of gp160

Fusion inhibition by binding to the N-terminal or C-terminal heptad repeat regions (HR1 or HR2) of gp41, thereby preventing the formation of the six-helix bundle required for viral-host membrane fusion.