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Herpes simplex virus-specific antigens are a diverse group of proteins encoded by the HSV-1 and HSV-2 genomes that play critical roles in the viral life cycle and serve as the primary targets for the host immune system [4, 13]. These antigens include envelope glycoproteins, such as gB, gC, gD, gH, and gL, which are essential for viral attachment and entry into host cells, as well as enzymes like thymidine kinase and DNA polymerase required for viral replication [2, 4, 13]. In the context of therapeutics, these antigens are targeted by a variety of agents, including nucleoside analogs (e.g., acyclovir) that inhibit DNA synthesis, helicase-primase inhibitors (e.g., pritelivir), and monoclonal antibodies that neutralize viral entry [1, 8, 9, 11]. Additionally, specific antigens like glycoprotein D and ICP4 have been the focus of subunit and live-attenuated vaccine development aimed at eliciting protective T-cell and B-cell responses [18, 19]. Understanding the function and immunogenicity of these antigens is vital for developing treatments that can manage symptomatic outbreaks, reduce viral shedding, and address the challenges of lifelong latency and emerging drug resistance [2, 12, 20].
Inhibition of viral DNA polymerase, inhibition of viral thymidine kinase, inhibition of viral helicase-primase complex, neutralization of viral entry by blocking glycoproteins, inhibition of viral fusion, and induction of antigen-specific immune responses via vaccines [1, 2, 8, 12].
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