Mumps virus fusion glycoprotein F (F protein)

The Mumps virus fusion glycoprotein F is a surface envelope protein of the mumps virus (family Paramyxoviridae, genus Rubulavirus)[1][4]. It is produced as an inactive precursor (F0) and activated by host cell proteases (such as furin) by cleavage into two subunits, F1 and F2, which are linked by disulfide bonds[4]. Structural studies show it forms a trimeric complex at the virus surface with two heptad repeat domains, assembling into a six-helix bundle upon triggering by receptor engagement of the hemagglutinin-neuraminidase (HN) protein[1][7][2]. This conformational change exposes a highly hydrophobic fusion peptide that inserts into the host cell membrane and mediates membrane merger at neutral pH[4]. The F protein is critical for viral entry, spread, and is a target for neutralizing antibodies induced by vaccination[9]. Variability in the F protein sequence (such as cleavage site or fusogenic domains) can affect virulence, cell tropism, and immune recognition[5][9]. Its structure and function are homologous to fusion proteins in other paramyxoviruses and are subject to ongoing vaccine research[2][8].

Other names

Mumps virus F proteinFusion proteinFusion glycoprotein F

Prevention of fusion and viral entry through neutralizing antibodies generated by vaccination Experimental fusion inhibitors could block conformational changes required for membrane fusion