Herpes Simplex Virus antigens (HSV antigens)

Herpes Simplex Virus (HSV) antigens refer to a diverse group of proteins encoded by the HSV-1 and HSV-2 genomes that serve as critical targets for both the host immune system and antiviral pharmacotherapy. These antigens primarily include surface glycoproteins such as gB, gD, and the gH/L complex, which facilitate viral attachment and entry into host cells, as well as essential replication enzymes like DNA polymerase (UL30) and the helicase-primase complex (UL5/UL8/UL52) [1, 2, 4]. In the context of infection, these proteins drive the viral life cycle, enabling the pathogen to establish lifelong latency in sensory neurons and periodically reactivate to cause mucocutaneous lesions, keratitis, or life-threatening encephalitis [12, 16]. Most current therapeutic interventions, such as acyclovir and foscarnet, target the viral DNA polymerase to halt replication through chain termination or enzyme inhibition [1, 3]. Emerging therapies, including pritelivir and amenamevir, target the helicase-primase complex to provide alternatives for drug-resistant strains [5, 6]. Additionally, surface glycoproteins are the primary focus of neutralizing monoclonal antibodies and subunit vaccine candidates aimed at preventing viral entry and reducing transmission [10, 13]. The characterization and targeting of HSV antigens remain central to overcoming clinical challenges like drug resistance and the persistent nature of latent viral reservoirs [9, 17].

Other names

Herpes simplex virus proteinsHSV-1 antigensHSV-2 antigensHSV surface glycoproteinsGlycoprotein B (gB)Glycoprotein D (gD)Glycoprotein H (gH)Glycoprotein L (gL)HSV DNA polymerase (UL30)HSV helicase-primase complex (UL5/UL8/UL52)

Inhibition of viral DNA polymerase through competitive substrate binding or pyrophosphate site blockade; inhibition of the viral helicase-primase complex; prevention of viral entry and membrane fusion; and immunological neutralization of virions by antibodies.