Herpes simplex virus 1 envelope glycoprotein C (gC-1)

Herpes simplex virus 1 (HSV-1) envelope glycoprotein C (gC-1) is a 511-amino-acid type I transmembrane protein that plays a dual role in viral infectivity and host immune evasion (UniProt P28986). It serves as the primary attachment factor for the virus, mediating the initial binding of the virion to cell surface heparan sulfate proteoglycans (PubMed: 1.3.1, 1.3.5). Beyond its role in entry, gC-1 is a critical immune modulator that binds to the host complement component C3b, thereby inhibiting the complement cascade and protecting the virus from neutralization and lysis (PubMed: 1.1.2, 1.3.2). Furthermore, gC-1 acts as a physical shield for other essential glycoproteins, such as gD and gB, preventing their recognition by neutralizing antibodies (BioRxiv: 1.1.1). Due to these multifaceted functions, gC-1 is a major target in the development of prophylactic and therapeutic vaccines, often as part of trivalent formulations designed to provide comprehensive protection against HSV-1 infection (PubMed: 1.3.2, 1.3.4).

Other names

gCUL44Envelope glycoprotein CGlycoprotein CHSV-1 gC

Inhibition of viral attachment to host cell heparan sulfate proteoglycans and blocking of complement-mediated immune evasion by preventing C3b binding.