Respiratory syncytial virus attachment glycoprotein G (RSV G protein)

Respiratory syncytial virus attachment glycoprotein G is a viral surface glycoprotein critical for the attachment of RSV to host respiratory epithelial cells. The G protein exists in two forms: a full-length membrane-bound form responsible for binding to multiple host molecules (including CX3CR1, glycosaminoglycans, surfactant A, annexin II, DC-SIGN, and L-SIGN) and a secreted form (sG) which acts as an immune decoy. The G protein is heavily glycosylated and contains a central conserved region with a CX3C motif that mimics the chemokine CX3CL1, enabling interaction with the chemokine receptor CX3CR1 but without receptor activation. This interaction facilitates viral attachment and modulates host immune responses, contributing to viral pathogenesis and immune evasion. RSV G is a target for vaccine and monoclonal antibody development, but most licensed interventions currently target the fusion (F) glycoprotein. The structure and function of conserved regions in G have enabled the development of neutralizing antibodies and inform next-generation RSV vaccine designs[1][3][5][6][7].

Other names

RSV G proteinRespiratory syncytial virus glycoprotein GRSV G glycoprotein

Blockade of RSV G attachment to CX3CR1 receptor, preventing viral entry\nNeutralization via antibody binding to conserved regions, inhibiting immune modulation and viral immune evasion[6][7].