Herpes simplex virus DNA primase (UL52) (UL52)

The Herpes simplex virus DNA primase (UL52) is the primase subunit of the heterotrimeric helicase-primase complex, which also includes the UL5 helicase and the UL8 scaffold protein [2, 11]. This complex is essential for viral DNA replication, where UL52 is responsible for synthesizing short RNA primers on the lagging strand to initiate DNA synthesis by the viral DNA polymerase [11, 13]. UL52 interacts extensively with UL5 and UL8 to coordinate the unwinding of double-stranded DNA and the subsequent primer synthesis at the replication fork [5, 13]. As a therapeutic target, UL52 is inhibited by a novel class of antiviral drugs known as helicase-primase inhibitors (HPIs), including pritelivir and amenamevir [1, 3, 10]. These inhibitors bind to the complex and stabilize its interaction with the DNA template, effectively halting the progression of the replication fork [2, 4, 24]. Because HPIs do not require activation by viral thymidine kinase and target a different mechanism than traditional nucleoside analogues like acyclovir, they are effective against drug-resistant HSV strains [1, 3, 14].

Other names

UL52pUL52HSV DNA primaseHerpes simplex virus type 1 protein UL52Herpes simplex virus type 2 protein UL52HSV-1 UL52HSV-2 UL52Primase subunit UL52

Helicase-primase inhibition; stabilization of the viral helicase-primase complex on DNA to prevent unwinding and primer synthesis [2, 4, 21, 24].