Herpes simplex virus type 1 virion proteins (HSV-1 proteins)

Herpes simplex virus type 1 (HSV-1) virion proteins comprise a complex assembly of structural and functional molecules essential for viral pathogenesis and replication [8, 14]. The virion is organized into four distinct layers: an inner core containing the double-stranded DNA genome, an icosahedral capsid (e.g., VP5), a protein-rich tegument (e.g., VP16, UL36), and an outer lipid envelope containing at least 11 glycoproteins (e.g., gB, gC, gD, gH, gL) [1, 8, 14]. Key therapeutic targets include the viral DNA polymerase (UL30), which is inhibited by nucleoside analogs like acyclovir after activation by the viral thymidine kinase (UL23) [3, 11, 13, 15]. Emerging targets include the helicase-primase complex (UL5/UL8/UL52), targeted by drugs like pritelivir and amenamevir, and the origin-binding protein (UL9/OBP) [2, 3, 4, 7]. These proteins facilitate critical steps such as host cell attachment, membrane fusion, genome replication, and immune evasion [1, 10, 21]. Resistance to standard therapies often involves mutations in the UL23 or UL30 genes, particularly in immunocompromised patients [13, 15, 16]. Safety concerns for drugs targeting these proteins include nephrotoxicity and the potential for cross-reactivity with host cell processes [3, 15].

Other names

HSV-1 structural proteinsHuman alphaherpesvirus 1 proteinsHSV-1 proteomeHerpes simplex virus type 1 proteins

Inhibition of viral DNA polymerase, viral DNA chain termination, inhibition of the helicase-primase complex, and inhibition of viral entry/fusion.