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Herpes simplex virus type 2 expresses multiple envelope glycoproteins critical to its infectivity and immune interactions. Among these, **glycoprotein C2 (gC2)** mediates virus attachment to host cell surfaces, primarily through interaction with heparan sulfate. **Glycoprotein D2 (gD2)** is essential for binding to specific host cell receptors and triggering membrane fusion required for virus entry. **Glycoprotein E2 (gE2)** forms a complex with glycoprotein I and plays a major role in evading host immune responses by binding to the Fc region of immunoglobulin G, interfering with antibody-mediated protection. All three are highly antigenic and elicit strong antibody responses during infection, making them key targets for diagnostic assays, vaccine development, and antiviral antibodies[3][6][7].
Vaccine antigens (stimulate protective immunity by inducing neutralizing antibodies against these glycoproteins) Monoclonal antibodies (block receptor binding and viral entry by targeting domain of gD2 or gC2)
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