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TitleMechanisms of HSV-1 helicase-primase inhibition and replication fork complex assembly.
Journal, issue, pagesCell, Vol. 189, Issue 2, Page 478-494.e18, Year 2026
Publish dateJan 22, 2026
AuthorsZishuo Yu / Pradeep Sathyanarayana / Cong Liu / Joel M J Tan / Pan Yang / Biswajit Das / Side Hu / Xiaoyi Fan / Chenggong Ji / Sandra K Weller / Mrinal Shekhar / Donald M Coen / Philip J Kranzusch / Joseph J Loparo / Jonathan Abraham /
PubMed AbstractHerpesviruses are widespread double-stranded DNA viruses that establish lifelong latency and cause various diseases. Although DNA-polymerase-targeting antivirals are effective, increasing drug ...Herpesviruses are widespread double-stranded DNA viruses that establish lifelong latency and cause various diseases. Although DNA-polymerase-targeting antivirals are effective, increasing drug resistance underscores the need for alternatives. Helicase-primase inhibitors (HPIs) are promising antivirals, but their mechanisms of action are poorly defined. Furthermore, how the helicase-primase (H/P) complex and DNA polymerase coordinate genome replication is not well understood for herpesviruses. Here, we report cryo-electron microscopy (cryo-EM) structures of the herpes simplex virus 1 H/P complex bound to HPIs, showing that these lock the H/P complex in an inactive state. Single-molecule assays reveal that HPIs cause H/P complexes to pause in unwinding activity on DNA. The structure of an HPI-bound replication fork complex, comprising the H/P complex (UL5, UL52, and UL8) and the polymerase holoenzyme (UL30 and UL42), reveals a previously uncharacterized interface bridging these complexes. These findings provide a structural framework for understanding herpesvirus replisome assembly and advancing inhibitor development.
External linksCell / PubMed:41468884 / PubMed Central
MethodsEM (single particle)
Resolution2.55 - 6.6 Å
Structure data

EMDB-72754: Local refinement of HSV UL5 in HSV replication fork complex
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-72755: Local refinement of HSV UL30 in HSV replication fork complex
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-72757: Low resolution map of HSV replication fork complex
Method: EM (single particle) / Resolution: 6.6 Å

EMDB-72758: Local refinement of interface of HSV UL5 and UL30 in the replication fork
Method: EM (single particle) / Resolution: 3.7 Å

72764

9yc9

EMDB-72764, PDB-9yc9:
HSV replication fork complex bound to pritelivir
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-72780: Local refinement of HSV UL5 in IM-250 bound H/P complex
Method: EM (single particle) / Resolution: 3.2 Å

72781

9ycp

EMDB-72781, PDB-9ycp:
HSV Helicase-primase complex bound to IM-250
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-72784: Local refinment of HSV UL5 in pritelivir-bound H/P complex
Method: EM (single particle) / Resolution: 3.35 Å

EMDB-72785: Local refinement of HSV UL8 in pritelivir-bound H/P complex
Method: EM (single particle) / Resolution: 3.3 Å

72786

9yct

EMDB-72786, PDB-9yct:
HSV helicase-primase complex bound to pritelivir
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-72787: Local refinement of HSV UL5 in amenamevir-bound H/P complex
Method: EM (single particle) / Resolution: 2.55 Å

EMDB-72788: Local refinement of HSV UL8 in amenamevir-bound H/P complex
Method: EM (single particle) / Resolution: 2.6 Å

72789

9ycv

EMDB-72789, PDB-9ycv:
HSV Helicase-primase complex bound to amenamevir
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-ZN:
Unknown entry

PDB-1bxb:
XYLOSE ISOMERASE FROM THERMUS THERMOPHILUS


PDB Unreleased entry

PDB-1chb: Unknown entry

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

Source
  • human alphaherpesvirus 1 strain r-15
KeywordsVIRAL PROTEIN / HSV / replisome / replication / helicase-primase complex / helicase-primase / pritelivir / HPI

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