Herpes simplex virus type 2 glycoprotein C (gC-2)

Herpes simplex virus type 2 glycoprotein C (gC-2) is a multifunctional type I integral membrane protein located on the viral envelope that is essential for pathogenesis (UniProt P03173). It functions as the primary attachment factor by binding to cell surface heparan sulfate proteoglycans, which initiates the tethering of the virus to host cells (Journal of Virology, 2022). Additionally, gC-2 acts as a potent immune evasion molecule by binding to host complement component C3b, thereby inhibiting the activation of the complement cascade and protecting the virus from neutralization and opsonization (PMC5465922). Due to its dual functionality in viral entry and immune suppression, gC-2 is a key component of next-generation multivalent vaccine candidates, such as the mRNA-1608 vaccine currently in clinical trials (Moderna, 2024). Targeting gC-2 aims to prevent viral adherence while simultaneously restoring the host's ability to clear the infection through complement-mediated immune mechanisms (PMC1900139).

Other names

gC2Envelope glycoprotein CGlycoprotein FUL44

The protein functions as a viral attachment factor by binding to host cell surface heparan sulfate and as an immune evasion molecule by binding host complement C3b (UniProt P03173). Therapeutic intervention involves blocking these interactions to prevent viral entry and restore complement-mediated neutralization of the virion (PMC5465922).