Respiratory Syncytial Virus G Glycoprotein (G glycoprotein)

The Respiratory Syncytial Virus (RSV) G glycoprotein is a major surface protein of the RSV virion, functioning primarily as the viral attachment protein. It mediates the initial binding of RSV to host cells, targeting ciliated epithelial cells in the human respiratory tract. The ectodomain contains two heavily glycosylated mucin-like regions separated by a central conserved, unglycosylated cysteine-rich "noose" stabilized by disulfide bonds. There are hypervariable segments at the C-terminal region of the ectodomain, contributing to antigenic diversity among strains. In immortalized cell lines it binds heparan sulfate proteoglycans (HSPG) and in airway epithelium models it interacts with CX3CR1. Both F and G proteins elicit neutralizing antibody responses during natural infection. G remains an important antigenic target because it acts as a neutralizing antigen and contributes significantly to immune evasion through its variability and heavy glycosylation shield.

Other names

RSV GAttachment protein GG protein

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