Evidence map›Paper›PMID 40543838›Full record

ArticleJournal of advanced research2026

Crotonylation driving Streptococcus pneumoniae adaption and virulence.

Nan Li, Jianpeng Zhuang, Jiayi Wu, Zhuoti Xue, Jiayi Xu, Zuye Fang, Yundan Zheng, Yun Liu, Yunpeng Yang, Xinyu Ye and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of advanced research, 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

12 authors.

Nan LiMOE Key Laboratory of Tumor Molecular Biology and State Key Laboratory of Bioactive Molecules and Druggability Assessment, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.
Jianpeng ZhuangMOE Key Laboratory of Tumor Molecular Biology and State Key Laboratory of Bioactive Molecules and Druggability Assessment, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.
Jiayi WuMOE Key Laboratory of Tumor Molecular Biology and State Key Laboratory of Bioactive Molecules and Druggability Assessment, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.
Zhuoti XueMOE Key Laboratory of Tumor Molecular Biology and State Key Laboratory of Bioactive Molecules and Druggability Assessment, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.
Jiayi XuMOE Key Laboratory of Tumor Molecular Biology and State Key Laboratory of Bioactive Molecules and Druggability Assessment, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.
Zuye FangMOE Key Laboratory of Tumor Molecular Biology and State Key Laboratory of Bioactive Molecules and Druggability Assessment, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.
Yundan ZhengMOE Key Laboratory of Tumor Molecular Biology and State Key Laboratory of Bioactive Molecules and Druggability Assessment, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.
Yun LiuMOE Key Laboratory of Tumor Molecular Biology and State Key Laboratory of Bioactive Molecules and Druggability Assessment, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.
Yunpeng YangMOE Key Laboratory of Tumor Molecular Biology and State Key Laboratory of Bioactive Molecules and Druggability Assessment, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.
Xinyu YeMOE Key Laboratory of Tumor Molecular Biology and State Key Laboratory of Bioactive Molecules and Druggability Assessment, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.
Qing-Yu HeMOE Key Laboratory of Tumor Molecular Biology and State Key Laboratory of Bioactive Molecules and Druggability Assessment, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China. Electronic address: tqyhe@jnu.edu.cn.
Xuesong SunMOE Key Laboratory of Tumor Molecular Biology and State Key Laboratory of Bioactive Molecules and Druggability Assessment, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China. Electronic address: tsunxs@jnu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

introductionTo cope with the host's stressful environment and immune clearance, some drug-resistant bacteria have reduced their virulence. Protein post-translational modifications (PTMs) are known to regulate numerous critical biological processes; however, their specific role in modulating bacterial virulence remains poorly understood.

objectiveThis study seeks to elucidate the mechanistic role of lysine crotonylation (Kcr) in modulating Streptococcus pneumoniae virulence and adaptive survival.

methodsThis study employed quantitative differential proteomics combined with animal models to delineate the critical role of Kcr in the adaptive survival of clinically multidrug-resistant bacterial strains. A crotonyltransferase was identified via knockout/overexpression screening, and its regulatory role was characterized using multi-omics characterization methods, including biochemical and molecular biology assays. Antibody-based enrichment coupled with proteomic techniques was utilized to map the enzyme-substrate network of the crotonyltransferase while comprehensive biochemical analyses-including isothermal titration calorimetry (ITC), hemolysis assays, immunoblotting, circular dichroism (CD) spectroscopy and molecular docking, deciphered its mechanism in modulating the virulence effector pneumolysin (PLY).

resultsOur results reveal that mice infected with clinically multidrug-resistant S.pn strains exhibit enhanced invasiveness but attenuated virulence. Quantitative proteomics reveal that Kcr serves as a critical regulator of bacterial virulence and host adaptation. SPD_0839 functions as a crotonyltransferase in S.pn, with Phe93 as its critical catalytic residue. SPD_0839 upregulates 205 Kcr sites on 153 substrates, enhancing the Kcr levels of key enzymes involved in energy metabolism, thereby regulating ATP production. Notably, SPD_0839 modulates the function of the key virulence factor PLY by catalyzing Kcr at Lys171 and Lys442, increases its pore-forming activity and ultimately enhances bacterial hemolysis activity and virulence.

conclusionOur findings shed light on the molecular mechanisms underlying PLY hemolytic activity regulated by Kcr, revealing its importance in bacterial survival and virulence. Overall, this research provides valuable insights into the important biological roles of Kcr in S.pn and offers potential theoretical foundations for developing new antibacterial drugs.

Indexed as

Pneumococcal InfectionsStreptococcus pneumoniaeAnimalsBacterial ProteinsDisease Models, AnimalLysineMiceProtein Processing, Post-TranslationalProteomicsStreptolysinsVirulenceBacterial ProteinsLysineplY protein, Streptococcus pneumoniaeStreptolysinsBacterial virulenceCrotonylationPneumolysinStreptococcus pneumoniae

Identifiers

PMID40543838
PMCPMC12957837

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.