HIV-1 envelope glycoprotein gp41 fusion peptide (gp41 fusion peptide (FP))

The HIV-1 envelope glycoprotein gp41 fusion peptide (FP) is a highly conserved, hydrophobic segment located at the N-terminus of the gp41 subunit of the envelope (Env) glycoprotein complex of human immunodeficiency virus type 1 (HIV-1)[1][2][5]. Upon binding of the virus to the CD4 receptor and a co-receptor (CCR5/CXCR4) on the host cell, conformational changes in another envelope subunit, gp120, trigger exposure of the gp41 fusion peptide[1][5]. The fusion peptide then inserts into the host cell membrane, enabling the viral and cellular membranes to come into close proximity and ultimately fuse[1][3][5]. The peptide is critical for the infectivity of HIV-1 and forms part of the "pre-hairpin intermediate" targeted by clinical and experimental HIV fusion inhibitors[3][5]. Synthetic peptides corresponding to the fusion peptide or to heptad repeat regions adjacent to it have demonstrated potent inhibition of HIV-1 infection, underscoring its central role as a therapeutic target[2][3]. Broadly neutralizing antibodies that recognize regions near the fusion peptide are key for vaccine research[5]. The gp41 fusion peptide is also notable for structural plasticity, facilitating complex conformational transitions required for fusion[1][4][5].

Other names

HIV-1 gp41 FPgp41 fusion peptideHIV-1 gp41 N-terminal fusion peptide

Fusion inhibitors bind to gp41 (including the fusion peptide or adjacent heptad repeat regions) to prevent conformational changes necessary for membrane fusion and viral entry[2][3].