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

The fusion glycoprotein of respiratory syncytial virus A, commonly referred to as the RSV F protein, is a surface membrane glycoprotein that mediates viral entry by catalyzing the fusion of the viral envelope with the membrane of host airway cells[1][3][7]. The F protein is synthesized as an inactive precursor (F0), which is cleaved into two subunits (F1 and F2) by host cell proteases[2]. In its functional state, the mature F protein is present as a trimer and undergoes major conformational rearrangements between prefusion and postfusion states, exposing the fusion peptide to trigger membrane fusion[4][5][7]. The RSV F protein is essential for infectivity, highly conserved among RSV strains, and the major target for neutralizing antibodies, making it a critical antigen for vaccine and monoclonal antibody development[1][3][6][7]. Antiviral drugs and preventative antibodies such as palivizumab and nirsevimab are designed to bind the F protein, particularly in the prefusion state, thereby preventing viral entry into host cells[7]. The F protein is a validated therapeutic target, central to RSV vaccine strategies, and its detection or immune response is used as a biomarker for RSV infection and vaccine efficacy[1][3][7]. Safety concerns include immune-mediated enhancement and antigenic variability affecting protective responses[7].

Other names

RSV fusion proteinF proteinRSV FViral fusion protein (RSV)Fusion glycoprotein (RSV)

Neutralization of virus by antibody binding to prefusion conformation; Inhibition of viral entry and fusion with host cell membrane; Vaccine-induced immune response