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Peer-reviewedCC BY-NC-ND 4.0Nature Communications

PARP10 condensation inhibits viral replication via targeting NAD+ homeostasis

  • Xiaoxin Chen1,2,3
  • Qi Xu2,3
  • Yi Liu2,3
  • Zhenshuo Zhu2,3
  • Ziqiu Wang2,3
  • Yun Zhang2,3
  • Ziru Li2,3
  • Yunan Mao2,3,4
  • Chenmiao Ai2,3
  • Qi Chen2,3
  • Le Tian2,3
  • Zhiying Yao2,3
3 more authors
  • Youngdae Gwon5
  • Zhubing Shi2,3
  • Peiguo Yang2,3,4
5 affiliations
  1. 1Fudan University, Shanghai, China
  2. 2State Key Laboratory of Gene Expression & Zhejiang Key Laboratory of Structural Biology, School of Life Sciences, Westlake University, Hangzhou, China
  3. 3Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, China
  4. 4School of Future Biomedicine, Westlake University, Hangzhou, China
  5. 5Department of Molecular Cell Biology, Sungkyunkwan University School of Medicine, Suwon, Republic of Korea
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Abstract

Although diphtheria toxin-like ADP-ribosyltransferases (ARTDs) are implicated in host-virus interactions, the specific antiviral mechanisms of certain family members remain largely undefined. Here, we reveal that mono-ADP-ribosyltransferase PARP10 restricts viral replication by forming biomolecular condensates via multivalent interactions among its structured domains. PARP10 condensates enhance enzymatic activity, resulting in increased NAD⁺ consumption that ultimately inhibits viral replication. The antiviral effects of PARP10 are shown to require both its catalytic activity and NAD⁺ regulation, as catalytic mutants and PARP10 inhibitors abrogate these effects, while reduction of NAD⁺ potently restricts viral replication. Furthermore, we identify auto-ADP-ribosylation as an intrinsic negative feedback mechanism modulating PARP10 condensation. These findings establish PARP10 condensation as a compartmentalization strategy that amplifies local NAD⁺ consumption to safeguard host antiviral immunity.

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Cite

BibTeXRIS
BibTeX
@article{chen2026parp10,
  title = {{PARP10 condensation inhibits viral replication via targeting NAD+ homeostasis}},
  author = {Xiaoxin Chen and Qi Xu and Yi Liu and Zhenshuo Zhu and Ziqiu Wang and Yun Zhang and Ziru Li and Yunan Mao and Chenmiao Ai and Qi Chen and Le Tian and Zhiying Yao and Youngdae Gwon and Zhubing Shi and Peiguo Yang},
  journal = {Nature Communications},
  year = {2026},
  month = sep,
  doi = {10.1038/s41467-026-78058-y},
  url = {https://doi.org/10.1038/s41467-026-78058-y},
  note = {CC BY-NC-ND 4.0},
}
RIS
TY  - JOUR
TI  - PARP10 condensation inhibits viral replication via targeting NAD+ homeostasis
AU  - Xiaoxin Chen
AU  - Qi Xu
AU  - Yi Liu
AU  - Zhenshuo Zhu
AU  - Ziqiu Wang
AU  - Yun Zhang
AU  - Ziru Li
AU  - Yunan Mao
AU  - Chenmiao Ai
AU  - Qi Chen
AU  - Le Tian
AU  - Zhiying Yao
AU  - Youngdae Gwon
AU  - Zhubing Shi
AU  - Peiguo Yang
PY  - 2026
DA  - 2026/09/26
JO  - Nature Communications
DO  - 10.1038/s41467-026-78058-y
UR  - https://doi.org/10.1038/s41467-026-78058-y
AB  - Although diphtheria toxin-like ADP-ribosyltransferases (ARTDs) are implicated in host-virus interactions, the specific antiviral mechanisms of certain family members remain largely undefined. Here, we reveal that mono-ADP-ribosyltransferase PARP10 restricts viral replication by forming biomolecular condensates via multivalent interactions among its structured domains. PARP10 condensates enhance enzymatic activity, resulting in increased NAD⁺ consumption that ultimately inhibits viral replication. The antiviral effects of PARP10 are shown to require both its catalytic activity and NAD⁺ regulation, as catalytic mutants and PARP10 inhibitors abrogate these effects, while reduction of NAD⁺ potently restricts viral replication. Furthermore, we identify auto-ADP-ribosylation as an intrinsic negative feedback mechanism modulating PARP10 condensation. These findings establish PARP10 condensation as a compartmentalization strategy that amplifies local NAD⁺ consumption to safeguard host antiviral immunity.
SN  - 2041-1723
ER  -