Fusion glycoprotein of human respiratory syncytial virus (RSV F protein)

The *fusion glycoprotein* (F protein) of human respiratory syncytial virus (RSV) is an integral viral surface protein essential for viral entry and pathogenesis[1][5][7]. Synthesized as a precursor (F0), it is proteolytically cleaved into two subunits (F1 and F2) linked by disulfide bonds; these associate as homotrimers in the viral envelope, cycling between a metastable pre-fusion (pre-F) and a stable post-fusion (post-F) conformation[2][5][6][7]. F mediates fusion of the viral and host cell membranes, enabling viral genome entry[7]. The pre-fusion F conformation presents unique neutralizing antibody epitopes and is the dominant antigenic target in natural infection and successful vaccines[7]. As a class I fusion protein, RSV F is highly conserved and is the target of licensed monoclonal antibody therapies as well as the first approved RSV vaccines. Its critical function and antigenicity make it a major therapeutic and vaccine target, particularly for preventing severe lower respiratory infections in infants and older adults[1][5][7].

Other names

F proteinFusion glycoproteinRSV FFusion (F) protein of RSV

Monoclonal antibodies bind to neutralizing epitopes on F (especially the pre-fusion conformation), preventing fusion of viral and cellular membranes and entry of virus into host cell[1][5][7]. Vaccines elicit neutralizing antibodies against the pre-fusion F protein to prevent infection[1][5][7].