Glycoprotein 41 subunit of envelope glycoprotein (gp41)

Glycoprotein 41 (gp41) is the transmembrane subunit of the HIV envelope spike complex, arising from proteolytic cleavage of the gp160 precursor into gp120 and gp41 by host cell proteases. Gp41 is anchored in the viral envelope and associates non-covalently with the surface-exposed gp120. Upon gp120 binding to CD4 and a coreceptor on the host cell, gp41 undergoes extensive conformational rearrangements that catalyze the fusion of viral and host cell membranes, a step essential for viral entry. Its structure contains a fusion peptide, two heptad repeat regions (NHR and CHR), a membrane proximal external region (MPER), and a transmembrane anchor. The highly conserved ectodomain and crucial role in membrane fusion make gp41 a validated target for antiretroviral therapy, specifically for fusion inhibitors such as enfuvirtide. Resistance is a concern in clinical use, and the development of peptide- and antibody-based therapies targeting gp41 continues as a priority for HIV research.

Other names

HIV envelope glycoprotein gp41HIV gp41HIV-1 envelope glycoprotein subunit gp41Transmembrane glycoprotein 41

Fusion inhibition: prevention of the formation of the six-helix bundle necessary for membrane fusion, thereby blocking HIV entry into host cells