Measles virus fusion glycoprotein (F0) (F)

The measles virus fusion glycoprotein (F0) is a type I transmembrane glycoprotein synthesized as an inactive precursor (F0) and cleaved by furin into F1 and F2 disulfide-linked subunits, exposing a fusion peptide for pH-independent membrane fusion after activation triggered by hemagglutinin (H) receptor binding. It undergoes irreversible conformational changes from a metastable prefusion trimeric state to a stable postfusion six-helix bundle (6HB) conformation, driving viral envelope-cell membrane fusion, syncytium formation, and nucleocapsid delivery. The protein features conserved domains including cytoplasmic tail, transmembrane region, fusion peptide, heptad repeats (HRA, HRB, HRC), and domains DI, DII, DIII; mutations in transmembrane or ectodomain regions modulate fusogenicity, complex formation with H, and inhibitor binding.[1][2][3][4][5][14]

Other names

fusion protein FF proteinMeV-Ffusion glycoprotein F0

Arrests prefusion F in intermediate state preventing postfusion transition, Binds hydrophobic pocket stabilizing prefusion conformation, Inhibits conformational changes required for fusion pore formation