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TitleStructural basis of herpesvirus helicase-primase inhibition by pritelivir and amenamevir.
Journal, issue, pagesSci Adv, Vol. 11, Issue 45, Page eadz1989, Year 2025
Publish dateNov 7, 2025
AuthorsAndrey G Baranovskiy / Qixiang He / Yoshiaki Suwa / Lucia M Morstadt / Nigar D Babayeva / Ci Ji Lim / Tahir H Tahirov /
PubMed AbstractWidespread herpesvirus infections are associated with various diseases. DNA replication of human herpes simplex virus type 1 (HSV-1) requires a helicase-primase (HP) complex of three core proteins: ...Widespread herpesvirus infections are associated with various diseases. DNA replication of human herpes simplex virus type 1 (HSV-1) requires a helicase-primase (HP) complex of three core proteins: UL5, UL52, and UL8. This complex unwinds viral DNA and synthesizes primers for DNA replication, making it an attractive antiviral target. Although HP inhibitors pritelivir and amenamevir were identified through screening, their binding mechanisms remain unclear. Here, we report cryo-electron microscopy structures of HSV-1 HP bound to a forked DNA template alone and in complex with pritelivir or amenamevir. The structures reveal a bilobed architecture highlighting HP coordinated action at the replication fork and providing a structural basis for HP inhibition by illustrating precisely how pritelivir and amenamevir block helicase activity. Data lay a solid foundation for the development of improved antiviral therapies.
External linksSci Adv / PubMed:41202142 / PubMed Central
MethodsEM (single particle)
Resolution2.86 - 3.43 Å
Structure data

EMDB-49560: Consensus map of HSV-1 helicase-primase in complex with a forked DNA and amenamevir
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-49561: Focused map of UL5-UL52 (C-terminal and N-terminal) of HSV-1 helicase-primase in complex with a forked DNA and amenamevir
Method: EM (single particle) / Resolution: 2.86 Å

EMDB-49562: Focused map of UL8-UL52(410-893) of HSV-1 helicase-primase in complex with a forked DNA and amenamevir
Method: EM (single particle) / Resolution: 2.96 Å

49563

9nn2

EMDB-49563, PDB-9nn2:
Composite structure of HSV-1 helicase-primase in complex with a forked DNA and amenamevir
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-49582: Consensus map of HSV1 helicase-primase in complex with a forked DNA
Method: EM (single particle) / Resolution: 3.43 Å

EMDB-49583: Focused map of UL5-UL52 (C-terminal and N-terminal) of HSV-1 helicase-primase in complex with a forked DNA
Method: EM (single particle) / Resolution: 3.16 Å

EMDB-49584: Focused map of UL8-UL52 (410-893) of HSV-1 helicase-primase in complex with a forked DNA
Method: EM (single particle) / Resolution: 3.18 Å

49585

9nnp

EMDB-49585, PDB-9nnp:
Composite structure of HSV-1 helicase-primase in complex with a forked DNA
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-49586: Consensus map of HSV-1 helicase-primase in complex with a forked DNA and pritelivir
Method: EM (single particle) / Resolution: 3.42 Å

EMDB-49587: Focused map of UL52-UL5 (C-terminal and N-terminal) of HSV-1 helicase-primase in complex with a forked DNA and pritelivir
Method: EM (single particle) / Resolution: 3.14 Å

EMDB-49588: Focused map of UL8-UL52 (417-890) of HSV-1 helicase-primase in complex with a forked DNA and pritelivir
Method: EM (single particle) / Resolution: 3.2 Å

49669

9nqp

EMDB-49669, PDB-9nqp:
Composite structure of HSV1 helicase-primase in complex with a forked DNA and pritelivir
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

PDB-1bxd:
NMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E. COLI OSMOSENSOR ENVZ

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

PDB-1bxb:
XYLOSE ISOMERASE FROM THERMUS THERMOPHILUS

Source
  • human alphaherpesvirus 1 strain 17
  • homo sapiens (human)
KeywordsTransferase/Hydrolase / DNA replication / HSV-1 helicase-primase / VIRAL PROTEIN / Transferase-Hydrolase complex / Transferase/Hydrolase/DNA / Transferase-Hydrolase-DNA complex / VIRAL PROTEIN/DNA / VIRAL PROTEIN-DNA complex

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