PLoS PathogensPharmacology & ToxicologyPeer-reviewed journal article
Viral Nuclease Inhibitors: Small molecule disruptors of the UL12 alkaline nuclease display broad anti-herpes virus activity
Nidhi Sharma, Xiaoyun Xie, Renata Szczepaniak, Chitra Rani, Sheida Khojasteh Khosro, J. KrucinskaiD, Xueao CheniD, Dung Do, Lee Wright, Dennis Wright, Sandra WelleriD
Abstract
Herpes simplex virus-1 (HSV-1) UL12 gene encodes a well-conserved 5 [->] 3 alkaline exonuclease. UL12 collaborates with the HSV single-strand DNA binding protein ICP8 to mediate recombination-dependent replication of viral DNA and is essential for the production of DNA that can be packaged into infectious virus. The UL12 gene has orthologs in the eight other human herpesviruses, including UL98 in HCMV and SOX in KSHV, which are also essential for virus production. We have developed viral nuclease inhibitors (VNIs) of HSV-1 UL12 that potently block its nuclease activity and display strong antiviral effects in cell culture. These inhibitors are also effective against alkaline nucleases from the {beta}-HHV HCMV (UL98) and the {gamma}-HHV KSHV (SOX), and we have demonstrated antiviral activity against HSV-1 and HCMV in cell culture. In this work, we describe the first crystal structure of an alphaherpesvirus alkaline nuclease (UL12.5), which was used to elucidate structure activity relationships and improve the selectivity of our inhibitors. These VNIs exhibit EC50 and IC50 values in the nanomolar to low micromolar range. Our findings highlight the potential of targeting HHV alkaline nucleases with novel small molecules, paving the way for the development of new therapies that can be broadly antiviral on their own or in combination with nucleoside analogs. Significance StatementHerpesviruses are widespread pathogens that establish lifelong infections and cause serious disease in immunocompromised individuals, neonates and older adults, yet treatment options remain limited. We report the first crystal structure of the HSV-1 alkaline nuclease UL12.5 and use it to design potent small-molecule inhibitors. These inhibitors exhibit antiviral activity against HSV-1 and HCMV, supporting alkaline nuclease as a conserved and druggable target across all herpesvirus subfamilies. The significance is threefold: it confirms alkaline nucleases as having an essential role in viral replication, provides a structural foundation for rational antiviral design and introduces a new class of inhibitors with potential as pan-herpesvirus therapeutics, alone or in combination, to overcome resistance and improve clinical outcomes.
- Citations
- 0
- FWCI
- 0.00
- Field percentile
- 39th percentile
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- LAVR-289, a new acyclo-nucleoside phosphonate having broad-spectrum activity against herpesviruses.
Sandrine Kappler‐Gratias, Charlotte Quentin-Froignant, … Franck Gallardo·bioRxiv·Feb 20, 2025
- Structural insights into inhibition mechanism of the helicase-primase complex from human herpesvirus 1
Ko Sato, Hisashi Ishida, … Toru Sengoku·Cell chemical biologyPeer-reviewed·Apr 15, 2026
- Virus-derived peptide inhibitors of the herpes simplex virus type 1 nuclear egress complex
E. B. Draganova, E. E. Heldwein·bioRxiv·Jun 24, 2020
- Mechanisms of HSV-1 helicase-primase inhibition and replication fork complex assembly
Zishuo Yu, Pradeep Sathyanarayana, … Jonathan Abraham·CellPeer-reviewed·Dec 29, 2025
- Structural Basis of Herpesvirus Helicase-Primase Inhibition by Pritelivir and Amenamevir
Andrey G. Baranovskiy, Qixiang He, … T.H. Tahirov·Science AdvancesPeer-reviewed·Nov 7, 2025
- Structure and mechanism of the HSV-1 origin-binding protein UL9
Cuiqing Huang, Haiqiang Wu, … Jun Ma·Journal of VirologyPeer-reviewed·Jul 10, 2026