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Herpes simplex virus type 2 (HSV-2) is a double-stranded DNA virus and a member of the Alphaherpesvirinae subfamily, primarily known as the causative agent of genital herpes [2, 11]. The virion is composed of a core containing the viral genome, an icosahedral capsid, a protein-rich tegument, and an outer lipid envelope containing essential glycoproteins [11, 18]. Key therapeutic targets within the virion include the viral DNA polymerase (UL30), which is the primary target for nucleoside analogs like acyclovir, and the helicase-primase complex, which is targeted by newer inhibitors such as pritelivir [3, 13]. Glycoproteins such as gD and gB facilitate viral attachment and membrane fusion, making them critical for infection and targets for entry inhibitors and vaccine development [4, 23]. HSV-2 is characterized by its ability to establish lifelong latent infections in sensory ganglia, from which it can periodically reactivate to cause recurrent lesions or asymptomatic shedding [2, 14]. While current antiviral treatments effectively suppress viral replication and reduce the severity of outbreaks, they do not eliminate the latent virus, presenting a significant challenge for long-term management and prevention of transmission [12, 14]. Additionally, HSV-2 infection is associated with an increased risk of HIV acquisition and can cause severe complications such as neonatal herpes and aseptic meningitis [11, 14].
DNA polymerase inhibition, Helicase-primase inhibition, Viral entry inhibition, Thymidine kinase-mediated activation
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