Respiratory syncytial virus fusion protein F (prefusion conformation, RSV B subtype) (RSV F (pre-F))

The Respiratory syncytial virus (RSV) fusion protein F is a critical surface glycoprotein that mediates viral entry into host respiratory epithelial cells (McLellan et al., Science, 2013). It exists in a metastable prefusion (pre-F) conformation on the virion surface, which, upon activation, undergoes a massive structural rearrangement into a stable postfusion (post-F) state to drive membrane fusion (Graham, Science, 2017). The pre-F conformation is the primary target for potent neutralizing antibodies because it displays highly sensitive epitopes, such as Site Ø, which are absent in the post-F form (Liang et al., Nature Communications, 2015). While RSV is divided into subtypes A and B, the F protein is relatively conserved (approx. 90% identity), though subtype-specific variations can influence the binding affinity of certain monoclonal antibodies and vaccines (Zhu et al., Science Translational Medicine, 2017). Therapeutic strategies focusing on the pre-F conformation, including monoclonal antibodies like nirsevimab and stabilized subunit vaccines like Arexvy and Abrysvo, aim to prevent infection and severe lower respiratory tract disease in infants and older adults (Hammitt et al., NEJM, 2022).

Other names

RSV fusion glycoproteinRSV-FPrefusion F proteinRSV B F proteinFusion protein F

Binding to the prefusion conformation of the F protein to prevent the structural transition to the postfusion state, thereby inhibiting viral-host membrane fusion and neutralizing the virus.