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

The Human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein gp41 subunit is a transmembrane protein that plays a critical role in the entry of the virus into host cells. It is derived from the proteolytic cleavage of the gp160 precursor polyprotein into the surface subunit gp120 and the transmembrane subunit gp41, which remain non-covalently associated on the viral surface (UniProt Q53I19). While gp120 is responsible for initial attachment to CD4 receptors and coreceptors (CCR5 or CXCR4), gp41 mediates the subsequent fusion of the viral and cellular membranes (PubMed: 22044225). This fusion process involves a dramatic conformational change where the N-terminal and C-terminal heptad repeat regions of gp41 fold into a stable six-helix bundle (6HB), bringing the membranes into close proximity for lipid mixing and pore formation (PubMed: 23344560). Because of its essential role in the viral life cycle, gp41 is a major therapeutic target for fusion inhibitors such as enfuvirtide, which bind to the transiently exposed regions of gp41 during the fusion process to block viral entry (Wikipedia).

Other names

Glycoprotein 41Transmembrane glycoprotein gp41TM subunitEnv gp41gp41 subunit of Env

Fusion inhibition by binding to the heptad repeat regions (NHR or CHR) of gp41, preventing the formation of the six-helix bundle (6HB) structure necessary for the fusion of viral and host cell membranes.