HIV-1 envelope glycoprotein gp41 (mediating membrane fusion) (gp41)

HIV-1 fusion describes the process by which the HIV-1 envelope glycoprotein complex, composed of gp120 and gp41, facilitates the merging of the viral and host cell membranes to allow viral entry. The primary molecular target for therapeutics in this context is the transmembrane subunit gp41, which undergoes major conformational changes upon receptor/co-receptor (CD4/CCR5 or CXCR4) engagement by gp120. This results in exposure and insertion of the gp41 fusion peptide into the host cell membrane, subsequent formation of a six-helix bundle, and ultimately fusion pore formation that allows viral genome transfer into the host cell[1][2][3][5][6]. Inhibitors such as enfuvirtide (T20) act by binding to regions of gp41, preventing six-helix bundle formation and blocking membrane fusion[3]. The target "HIV-1 fusion" is ambiguous and non-canonical, since it refers to a biological process; the actual therapeutic target is specifically "HIV-1 envelope glycoprotein gp41".

Other names

HIV-1 fusion proteinenvelope fusion subunitEnv fusion peptidegp41 fusion intermediate

Inhibition of six-helix bundle formation (fusion inhibitor)