Evidence map›Paper›PMID 40239620›Full record

ArticleCell reports. Medicine2025

Herpes simplex virus 1 encodes a STING antagonist that can be therapeutically targeted.

An Wang, Qianqian Peng, Huidi Fan, Wenting Ji, Jing Lou, Xi Zhou, Yujie Ren

Abstract read
In one paragraph

Article in Cell reports. Medicine, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. The COX2-PGEbioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

An WangState Key Laboratory of Virology and Biosafety, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China; University of Chinese Academy of Sciences, Beijing 100049, China.
Qianqian PengState Key Laboratory of Virology and Biosafety, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China.
Huidi FanState Key Laboratory of Virology and Biosafety, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China; School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230026, China.
Wenting JiState Key Laboratory of Virology and Biosafety, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China; School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230026, China.
Jing LouState Key Laboratory of Virology and Biosafety, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China.
Xi ZhouState Key Laboratory of Virology and Biosafety, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China; University of Chinese Academy of Sciences, Beijing 100049, China; School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230026, China. Electronic address: zhouxi@wh.iov.cn.
Yujie RenState Key Laboratory of Virology and Biosafety, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China; University of Chinese Academy of Sciences, Beijing 100049, China. Electronic address: renyujie@wh.iov.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Herpes simplex virus 1 (HSV-1) is a ubiquitous human pathogen that causes serious symptoms and is known for its strong interactions with host immunity. Here, we revealed that the HSV-1-encoded UL38 is a stimulator of interferon genes (STING) antagonist that interacts with STING to abrogate the STING-TANK-binding kinase 1 (TBK1)-interferon regulatory factor 3 (IRF3) interaction, thereby suppressing cyclic GMP-AMP synthase (cGAS)-STING-dependent immune signaling. Losing UL38's STING antagonist activity made HSV-1 incapable of immune evasion and less replicable and pathogenic in vivo. Moreover, on the basis of the UL38-interacting sequence within STING, we rationally designed a series of peptides to target the STING-UL38 interface of UL38 specifically. Among them, a peptide effectively disrupts the STING-UL38 interaction, which unlocks the UL38-suppressed immune response and shows potent therapeutic efficacy against HSV-1 infection in vivo. Therefore, our findings demonstrate that HSV-1 UL38 is a STING antagonist, and targeting the activity of UL38 is a promising strategy for the development of antivirals against this notorious virus.

Indexed as

Herpesvirus 1, HumanMembrane ProteinsViral ProteinsAnimalsAntiviral AgentsChlorocebus aethiopsFemaleHEK293 CellsHerpes SimplexHumansInterferon Regulatory Factor-3MiceNucleotidyltransferasesProtein BindingProtein Serine-Threonine KinasesSignal TransductionAntiviral AgentsInterferon Regulatory Factor-3Membrane ProteinsNucleotidyltransferasesProtein Serine-Threonine KinasesSTING1 protein, humanSTING ProteinViral Proteinsantiviral innate immunityantiviralsdrug targetherpes simplex virus 1STINGUL38

Identifiers

PMID40239620
PMCPMC12047521

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.