Respiratory syncytial virus fusion glycoprotein (RSV F) (RSV F)

The Respiratory syncytial virus (RSV) fusion (F) glycoprotein is a type I integral membrane protein that plays a pivotal role in the viral entry process by mediating the fusion of the viral envelope with the host cell plasma membrane (PubMed: 23640882). It is synthesized as a precursor, F0, which is proteolytically cleaved into F1 and F2 subunits that form a functional homotrimer. Antigenic site A, frequently referred to as Site II, is a highly conserved conformational epitope located on the F1 subunit and is accessible in both the metastable pre-fusion and the stable post-fusion conformations of the protein (PubMed: 2612447, 10482726). This site is the target of palivizumab, a humanized monoclonal antibody used for the prevention of severe lower respiratory tract disease caused by RSV in high-risk infants (PubMed: 9371549). By binding to Site II, therapeutic antibodies inhibit the structural transitions of the F protein necessary for membrane fusion, effectively neutralizing the virus and preventing infection of host cells (PubMed: 21690342). Because of its essential role in the viral life cycle and its conservation across RSV strains, the F protein, and specifically Site II, remains a primary focus for passive immunoprophylaxis and vaccine development.

Other names

Antigenic site IISite IISite ARSV F proteinFusion proteinRespiratory syncytial virus fusion glycoprotein, antigenic site A

Binds to antigenic site II (Site A) of the RSV F protein and prevents the conformational change from the pre-fusion to the post-fusion state required for viral-host membrane fusion (PubMed: 23640882, 10482726).