Evidence map›Paper›PMID 41144710›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026

Blocking Lysine Crotonylation and Aerobic Glycolysis as Targeting Strategy Against mpox Virus Replication.

Pengjun Wei, Zongzheng Zhao, Ruoqi Xu, Qin Yan, Liangzi Jiang, Fuxiao Geng, Yang Gu, Tianjiao Wang, Jing Zhou, Xiao Li and 3 more

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

13 authors.

Pengjun WeiDepartment of Microbiology, Nanjing Medical University, Nanjing, 211166, P. R. China.
Zongzheng ZhaoChangchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Changchun, 130122, P. R. China.
Ruoqi XuDepartment of Microbiology, Nanjing Medical University, Nanjing, 211166, P. R. China.
Qin YanDepartment of Microbiology, Nanjing Medical University, Nanjing, 211166, P. R. China.
Liangzi JiangDepartment of Microbiology, Nanjing Medical University, Nanjing, 211166, P. R. China.
Fuxiao GengDepartment of Microbiology, Nanjing Medical University, Nanjing, 211166, P. R. China.
Yang GuDepartment of Microbiology, Nanjing Medical University, Nanjing, 211166, P. R. China.
Tianjiao WangDepartment of Microbiology, Nanjing Medical University, Nanjing, 211166, P. R. China.
Jing ZhouDepartment of Microbiology, Nanjing Medical University, Nanjing, 211166, P. R. China.
Xiao LiChangchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Changchun, 130122, P. R. China.
Qin YanDepartment of Microbiology, Nanjing Medical University, Nanjing, 211166, P. R. China.
Chun LuDepartment of Microbiology, Nanjing Medical University, Nanjing, 211166, P. R. China.
Wan LiDepartment of Microbiology, Nanjing Medical University, Nanjing, 211166, P. R. China.ORCID https://orcid.org/0000-0001-5675-2429

Funding

Changzhou Medical Center CMC2024PY02National Key R&D Program 2023YFC2306600National Natural Science Foundation of China 32170151National Natural Science Foundation of China 32570171National Natural Science Foundation of China 82172262National Natural Science Foundation of China 82241067National Natural Science Foundation of China 82372243National Natural Science Foundation of China 82572562Natural Science Foundation of Jiangsu Province BK20240133
6 · The paper itself

Abstract

The global outbreak of mpox caused by the mpox virus (MPXV) in 2022 and 2024 underscores the urgent need to elucidate mechanisms governing viral replication during pathogenesis. Metabolic reprogramming is a conserved hallmark of viral infections, however, the precise mechanisms by which MPXV manipulates host cell metabolism remain unknown. Here, it is demonstrated that MPXV hijacks aerobic glycolysis via lysine crotonylation of its I3 protein, which is essential for MPXV replication. Mechanistically, MYST histone acetyltransferase 1 (MYST1), an acetyltransferase upregulated by MPXV, binds to and catalyzes the crotonylation of I3. The crotonylated I3 interacts with WD-repeat protein 26 (WDR26) to prevent its ubiquitination-dependent degradation, leading to enhanced aerobic glycolysis and promoting MPXV replication. Either pharmacological inhibition of MYST1 using MC4033 or blocking aerobic glycolysis with the glycolytic inhibitors 2-Deoxy-D-glucose (2-DG) or dichloroacetic acid (DCA) effectively suppresses MPXV replication. These findings uncover a novel crotonylation-dependent mechanism through which MPXV reprograms host metabolism to facilitate viral propagation, and identify lysine crotonylation and aerobic glycolysis as potential therapeutic targets against mpox.

Indexed as

GlycolysisLysineMonkeypox virusVirus ReplicationAnimalsHistone AcetyltransferasesHumansHistone AcetyltransferasesLysineaerobic glycolysiscrotonylationI3mpox virusMYST1

Identifiers

PMID41144710
PMCPMC12822389

What OpenQuestion holds

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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.