Evidence map›Paper›PMID 42045228›Full record

ArticleNature communications2026

Reprogramming of bacterial virulence by lysine acetylation.

Ole Schmöker, Britta Girbardt, Sabrina Schulze, Gottfried J Palm, Leona Berndt, Jens Hoppen, Nilüfer Kara, Xenia Schöps, Ruba Al-Abdulla, Klara Garz and 19 more

Abstract read
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In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

29 authors.

Ole SchmökerDepartment Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.ORCID 0009-0005-4754-8246
Britta GirbardtDepartment Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.
Sabrina SchulzeDepartment Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.ORCID 0000-0002-0122-5688
Gottfried J PalmDepartment Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.ORCID 0000-0003-0329-0413
Leona BerndtDepartment Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.
Jens HoppenDepartment Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.
Nilüfer KaraDepartment Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.ORCID 0000-0002-6618-379X
Xenia SchöpsDepartment Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.
Ruba Al-AbdullaInstitute of Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Greifswald, Germany.ORCID 0000-0002-5194-9801
Klara GarzInstitute of Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Greifswald, Germany.
Heike JunkerInstitute of Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Greifswald, Germany.
Sophie WolfgrammInstitute of Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Greifswald, Germany.ORCID 0009-0004-0353-6457
Leif SteilInterfaculty Institute for Genetics and Functional Genomics, University of Greifswald, University Medicine Greifswald, Greifswald, Germany.ORCID 0000-0002-0733-8421
Christian HentschkerInterfaculty Institute for Genetics and Functional Genomics, University of Greifswald, University Medicine Greifswald, Greifswald, Germany.
Katrin SchoknechtInterfaculty Institute for Genetics and Functional Genomics, University of Greifswald, University Medicine Greifswald, Greifswald, Germany.
Lea-Maria MayerDepartment of Microbiology, University of Würzburg, Biocenter, Würzburg, Germany.ORCID 0009-0007-5123-9854
Leonie SpethDepartment of Microbiology, University of Würzburg, Biocenter, Würzburg, Germany.ORCID 0009-0000-9507-0113
Vanessa LachmayerInstitute for Genetics, University of Cologne, Cologne, Germany.
Mark DörrDepartment Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.ORCID 0000-0003-3270-6895
Stefan KemnitzDepartment for High Performance Computing, University of Greifswald, University Computing Center, Greifswald, Germany.
Stefan MüllerInstitute for Genetics, University of Cologne, Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), Cologne, Germany.
Jan-Wilm LackmannInstitute for Genetics, University of Cologne, Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), Cologne, Germany.ORCID 0000-0001-8182-8034
Marcus KrügerInstitute for Genetics, University of Cologne, Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), Cologne, Germany.ORCID 0000-0002-5846-6941
Kay HofmannInstitute for Genetics, University of Cologne, Cologne, Germany.ORCID 0000-0002-2289-9083
Uwe T BornscheuerDepartment Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.ORCID 0000-0003-0685-2696
Uwe VölkerInterfaculty Institute for Genetics and Functional Genomics, University of Greifswald, University Medicine Greifswald, Greifswald, Germany.ORCID 0000-0002-5689-3448
Elke KrügerInstitute of Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Greifswald, Germany.ORCID 0000-0002-2551-242X
Vera Kozjak-PavlovicDepartment of Microbiology, University of Würzburg, Biocenter, Würzburg, Germany.ORCID 0000-0001-9658-7018
Michael LammersDepartment Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany. michael.lammers@uni-greifswald.de.ORCID 0000-0003-4168-4640

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) 441529220Deutsche Forschungsgemeinschaft (German Research Foundation) 443535983Deutsche Forschungsgemeinschaft (German Research Foundation) 445120888
6 · The paper itself

Abstract

Gram-negative bacteria use a plethora of virulence factors to infect eukaryotic cells. CE-clan protease-related virulence factors were reported to act as deubiquitinases/ubiquitin-like specific proteases. Some have an additional acetyl-transferase activity. The molecular mechanisms underlying this dual activity and the physiological consequences are only marginally understood. Here, we report crystal structures for the Simkania negevensis virulence factor SnCE1 in apo-states and in complex with SUMO1. We confirm SnCE1 acting as an efficient deSUMOylase and discover an intrinsic autoacetyltransferase activity. Acetylation impairs SnCE1 tetramer formation structurally being incompatible with SUMO1 binding. We provide a model for regulation of SnCE1-mediated virulence by lysine acetylation modulating autoproteolytic processing and its subcellular distribution in the host cell. SnCE1 localizes to the endoplasmic reticulum in human cells and increases fragmentation of mitochondria. Our data provide mechanistic insights into how lysine acetylation of virulence factors is used to reprogram virulence adjusting it to the host cells' metabolic state.

Indexed as

Bacterial ProteinsLysineVirulence FactorsAcetylationCrystallography, X-RayEndoplasmic ReticulumHumansModels, MolecularSUMO-1 ProteinVirulenceBacterial ProteinsLysineSUMO-1 ProteinVirulence Factors

Identifiers

PMID42045228
PMCPMC13125535

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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.