Respiratory syncytial virus fusion protein (RSV PreF) (RSV PreF)

The Respiratory syncytial virus (RSV) fusion (F) protein is a class I viral fusion glycoprotein that is essential for viral entry into host cells by mediating the fusion of the viral envelope with the host cell membrane (McLellan et al., 2013). It exists in a metastable prefusion (pre-F) conformation and a stable postfusion (post-F) conformation; the pre-F form is the primary target for potent neutralizing antibodies because it contains highly sensitive epitopes, such as Site Ø, which are absent in the post-F form (Graham, 2011). Targeting the prefusion conformation is the basis for modern RSV prevention strategies, including the monoclonal antibody nirsevimab and the vaccines Arexvy and Abrysvo (Hammitt et al., 2022; Papi et al., 2023). These therapeutics work by binding to the pre-F protein on the surface of RSV A and B virions, thereby preventing the structural rearrangement into the post-F state that is required for membrane fusion and subsequent infection of respiratory epithelial cells (McLellan et al., 2013). This target is clinically significant for reducing the burden of bronchiolitis and pneumonia in vulnerable populations, particularly infants and the elderly (Walsh et al., 2023).

Other names

RSV F proteinPrefusion FRSV fusion glycoproteinRSV-FFusion protein F0

Neutralization of the virus by binding to the prefusion conformation of the F protein, which prevents the irreversible conformational change to the postfusion state required for the fusion of viral and host cell membranes (McLellan et al., 2013; Hammitt et al., 2022).