Herpes simplex virus glycoprotein C (gC)

Herpes simplex virus glycoprotein C (gC) is a multifunctional type I integral membrane protein located on the viral envelope of both HSV-1 and HSV-2. It serves as the primary attachment ligand for the virus, mediating initial binding to host cell surface heparan sulfate and chondroitin sulfate proteoglycans. Beyond its role in entry, gC is a critical immune evasion factor that functions as a receptor for the host complement component C3b, thereby inhibiting the alternative complement pathway and protecting the virus from complement-mediated neutralization. In addition to its direct roles, gC acts as a physical shield for other essential glycoproteins, such as gB and gD, protecting them from neutralizing antibodies. It also facilitates viral entry through low-pH endosomal pathways by modulating the conformational transitions of the fusion protein gB. Because of its diverse roles in attachment and immune evasion, gC is a prominent target in the development of next-generation subunit vaccines and monoclonal antibody therapies aimed at preventing or treating herpes simplex infections.

Other names

Envelope glycoprotein CgC-1gC-2UL44Glycoprotein F

Inhibition of viral attachment to cell surface glycosaminoglycans, blockade of complement evasion by preventing C3b binding, and neutralization of viral entry by interfering with gC-mediated conformational changes in the fusion protein gB.