Respiratory syncytial virus attachment glycoprotein and fusion glycoprotein (RSV G and F proteins)

The respiratory syncytial virus attachment glycoprotein (G) and fusion glycoprotein (F) are the principal surface proteins of RSV, a major human respiratory pathogen. The G protein mediates viral attachment to host epithelial cells by binding cellular receptors such as CX3CR1 and glycosaminoglycans. It exists in membrane-bound and secreted forms, the latter modulating immune responses and functioning as an antibody decoy[3][4][5]. The F protein is a class I fusion protein that drives fusion of the viral and host membranes, a critical step for viral entry and propagation. F is highly conserved, a main target for neutralizing antibodies, and the focus of nearly all licensed and investigational therapeutic monoclonal antibodies and vaccines[1][2][4][5]. Both proteins are essential for RSV infectivity and pathogenesis, with the F protein being indispensable for viral fusion and the G protein chiefly enhancing host cell interaction and modulating immune responses. Drugs that target these proteins, particularly F, are effective in preventing or ameliorating RSV infection, while ongoing research continues to exploit them as key antigens for vaccine and therapeutic development[1][4][5].

Other names

RSV G proteinRSV F proteinRSV attachment glycoprotein (G)RSV fusion glycoprotein (F)Respiratory syncytial virus GRespiratory syncytial virus F

Neutralizing antibodies prevent viral entry by blocking F protein–mediated fusion Antibodies to G can block viral attachment to host cell surface Inhibition of F-mediated membrane fusion Interference with G protein–mediated host receptor interactions (e.g., CX3CR1), reducing both viral attachment and immune modulation