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Herpes simplex virus 1 glycoprotein C (gC) is a multifunctional type I transmembrane protein located in the viral envelope. It plays a critical role in the initial stages of infection by mediating the attachment of the virus to host cell surface heparan sulfate proteoglycans (1.1.2, 1.4.2). Beyond attachment, gC is a key player in immune evasion; it binds to the C3b component of the host complement system, thereby inhibiting complement-mediated neutralization and lysis of infected cells (1.1.2, 1.4.3). It also acts as a physical shield for other essential glycoproteins like gB and gD, protecting them from neutralizing antibodies (1.4.3, 1.4.5). Because of these roles, gC is a prominent target in the development of vaccines and antiviral therapies aimed at blocking viral entry and enhancing the host's immune response (1.1.1, 1.4.3). Experimental treatments include heparan sulfate mimetics like PI-88 and monoclonal antibodies that disrupt its binding capabilities (1.2.1, 1.4.4).
Inhibition of viral attachment to heparan sulfate proteoglycans and blockade of complement-mediated immune evasion.
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