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Structure paper

TitleStructural and mechanistic insights into herpesvirus helicase-primase and its therapeutic inhibitors.
Journal, issue, pagesNat Microbiol, Vol. 10, Issue 12, Page 3191-3201, Year 2025
Publish dateNov 4, 2025
AuthorsQing Yao / Alexandre Mercier / Arabinda Nayak / Lindsey May / Pui Yan Ho / Ariel Lewis-Ballester / Varsha Nair / Annapurna Sapre / Thomas Aeschbacher / Jit Mukherjee / Christopher Richards / Roberto Mateo / Aesop Cho / Eric Lansdon / Xinchao Yu /
PubMed AbstractThe herpes simplex virus (HSV) helicase-primase (HP) complex is a promising anti-herpes therapeutic target. However, progress in developing highly effective small-molecule HP inhibitors (HPIs) for ...The herpes simplex virus (HSV) helicase-primase (HP) complex is a promising anti-herpes therapeutic target. However, progress in developing highly effective small-molecule HP inhibitors (HPIs) for the treatment of genital herpes has been hindered by the lack of structural information on the HP complex and the incomplete understanding of the mechanism of action of HPIs. Here we present the cryogenic electron microscopy structure of the HSV-1 HP apo-complex (3.8 Å), along with structures bound to pritelivir (3.2 Å) and amenamevir (3.2 Å)-two clinically active, chemically distinct HPIs. The potency of both inhibitors against HSV variants bearing mutations within the HPI binding pocket supports the high-resolution mapping of key molecular interactions while revealing residues that govern their antiviral spectrum against alphaherpesviruses. Our results provide important insight into the unique architecture of the HP complex and the mechanism of inhibition of HPIs, paving the way for the development of next-generation antivirals to treat herpesvirus infections.
External linksNat Microbiol / PubMed:41188384 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.8 Å
Structure data

49269

9nda

EMDB-49269, PDB-9nda:
The rigid portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex with amenamevir
Method: EM (single particle) / Resolution: 2.9 Å

49276

9ndq

EMDB-49276, PDB-9ndq:
The rigid portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex prepared with forked DNA and ATP-gamma-S
Method: EM (single particle) / Resolution: 3.0 Å

49277

9ndt

EMDB-49277, PDB-9ndt:
The flexible portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex prepared with forked DNA and ATP-gamma-S
Method: EM (single particle) / Resolution: 3.8 Å

49290

9ndz

EMDB-49290, PDB-9ndz:
The rigid portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex prepared with forked DNA, ATP-gamma-S and Pritelivir
Method: EM (single particle) / Resolution: 3.0 Å

49291

9ne0

EMDB-49291, PDB-9ne0:
The flexible portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex prepared with forked DNA, ATP-gamma-S and Pritelivir
Method: EM (single particle) / Resolution: 3.4 Å

49304

9neb

EMDB-49304, PDB-9neb:
The rigid portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex with Pritelivir
Method: EM (single particle) / Resolution: 2.8 Å

49306

9nee

EMDB-49306, PDB-9nee:
The flexible portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex with Pritelivir
Method: EM (single particle) / Resolution: 3.2 Å

49326

9nel

EMDB-49326, PDB-9nel:
The flexible portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex with amenamevir
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

PDB-1bxb:
XYLOSE ISOMERASE FROM THERMUS THERMOPHILUS

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

Source
  • herpesviridae (virus)
KeywordsREPLICATION / TRANSFERASE / Inhibitor / Helicase / Primase / Herpesvirus / Forked DNA / Pritelivir / TRANSFERASE/INHIBITOR / TRANSFERASE-INHIBITOR complex

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