Respiratory syncytial virus attachment glycoprotein (G) (RSV G)

The Respiratory syncytial virus attachment glycoprotein (G) is a type II transmembrane protein located on the surface of the Respiratory Syncytial Virus (RSV) virion. Its primary biological function is the initial attachment to host ciliated airway epithelial cells by binding to glycosaminoglycans like heparan sulfate and the host CX3C chemokine receptor 1 (CX3CR1). The protein is unique for existing in both membrane-bound and secreted forms; the latter acts as an immunological decoy, neutralizing host antibodies before they can reach the viral particle. In disease states, the G protein plays a significant role in pathogenesis by modulating the host immune response. Its central conserved domain contains a CX3C chemokine motif that mimics host fractalkine, allowing the virus to interfere with immune cell trafficking and suppress the production of protective type I and III interferons. While currently approved monoclonal antibodies like Palivizumab and Nirsevimab target the fusion (F) protein, the G protein is an emerging therapeutic target for next-generation monoclonal antibodies (such as 3D3 and 2D10) and subunit vaccines designed to restore host antiviral immunity and block viral entry.

Other names

Attachment glycoprotein GG proteinGlycoprotein GMajor surface glycoprotein GRespiratory syncytial virus G protein

Neutralization of viral attachment and inhibition of G protein-mediated immune modulation by blocking CX3C-CX3CR1 receptor interactions and restoring host interferon responses.