RSV F glycoprotein (RSV F)

The RSV F glycoprotein is a type I membrane protein on the surface of respiratory syncytial virus that mediates viral entry into host cells by catalyzing membrane fusion. It is synthesized as an inactive precursor (F0) and activated by host protease cleavage, yielding F1 and F2 subunits linked by disulfide bonds. The active fusion protein exists as a homotrimer in a metastable prefusion conformation, triggering dramatic structural rearrangement upon activation to enable fusion. RSV F is the primary target for neutralizing antibodies and for vaccine and antiviral drug development, with licensed vaccines and monoclonal antibodies directly targeting its prefusion state. The target is specific and correctly identified in the context of infection and respiratory disease.

Other names

RSV Fusion proteinF proteinFusion glycoproteinRSV F

Neutralizing antibodies bind exposed epitopes on prefusion or postfusion RSV F, preventing the conformational change necessary for membrane fusion, thereby blocking viral entry into host cells. Vaccine antigens elicit protective immune responses—mainly neutralizing antibodies targeting antigenic sites on prefusion F.