Respiratory syncytial virus glycoprotein G (RSV G) and Respiratory syncytial virus fusion glycoprotein (RSV F) (RSV G, RSV F)

Respiratory syncytial virus (RSV) antigens most commonly refer, in the context of therapeutic targeting, to the virus’s two main surface glycoproteins: the attachment glycoprotein (G) and the fusion glycoprotein (F). The G protein mediates viral attachment to ciliated epithelial cells of the airways primarily through interaction with the host receptor CX3CR1, while the F protein promotes viral and cell membrane fusion, a key step in infection. Both F and G are primary targets for neutralizing antibodies, vaccine candidates, and therapeutic monoclonal antibodies. The F protein, in particular, is the current focus of most prophylactic drug and vaccine efforts (e.g., palivizumab, nirsevimab), due to its role in cell entry and as a highly conserved target of neutralizing antibody responses. The G protein’s functions additionally include immune evasion through decoy mechanisms (the secreted form sG) and immune modulation. Though G is a bona fide target, it is less commonly targeted therapeutically due to variable immunogenicity and safety concerns in the context of vaccine enhancement[1][2][3][4][5][6][7].

Other names

G glycoproteinAttachment glycoproteinRSV F proteinFusion glycoprotein

Inhibition of viral entry (fusion or attachment blockade); Neutralization by binding viral surface proteins, preventing host infection; Interference with protein–receptor interactions (e.g., G binding to CX3CR1)