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Cited by 2Ubiquitin and proteasome pathwaysEnzyme Structure and FunctionBacterial Genetics and Biotechnology

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Reprogramming of bacterial virulence by lysine acetylation

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Schmöker, Ole, Girbardt, Britta, Schulze, Sabrina, Palm, Gottfried J., Berndt, Leona, Hoppen, Jens, Kara, Nilüfer, Schöps, Xenia, Al-Abdulla, Ruba, Garz, Klara, Junker, Heike, Wolfgramm, Sophie, Steil, Leif, Hentschker, Christian, Schoknecht, Katrin, Mayer, Lea-Maria, Speth, Leonie, Lachmayer, Vanessa, Dörr, Mark, Kemnitz, Stefan, Müller, Stefan, Lackmann, Jan-Wilm, Krüger, Marcus, Hofmann, Kay, Bornscheuer, Uwe T., Völker, Uwe, Krüger, Elke, Kozjak-Pavlovic, Vera, Lammers, Michael·2026·Nature Communications
DOI 10.1038/s41467-026-72244-8

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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.

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Metadata

Authors
Schmöker, O., Girbardt, B., Schulze, S., Palm, G. J., Berndt, L., Hoppen, J., Kara, N., Schöps, X., Al-Abdulla, R., Garz, K., Junker, H., Wolfgramm, S., Steil, L., Hentschker, C., Schoknecht, K., Mayer, L.-M., Speth, L., Lachmayer, V., Dörr, M., Kemnitz, S., Müller, S., Lackmann, J.-W., Krüger, M., Hofmann, K., Bornscheuer, U. T., Völker, U., Krüger, E., Kozjak-Pavlovic, V., & Lammers, M.
Affiliations
  • Universität Greifswald (DE)
  • Universitätsmedizin Greifswald (DE)
  • University of Würzburg (DE)
  • University of Cologne (DE)
Corresponding author
Lammers, Michael
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2026-04-27
Volume
17
Issue
1
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-026-72244-8
OpenAlex
W7155847512
Cited by
2
References
2
Citations by year
2026: 2
FWCI
4.13
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • Research Square (acceptedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
Deutsche Forschungsgemeinschaft (443535983, 445120888, 441529220)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords
lysine acetylation, bacterial virulence, Simkania negevensis, SUMO1, protein crystal structure, tetramer formation, endoplasmic reticulum localization, mitochondrial fragmentation, host cell metabolism, Gram-negative bacteria
MeSH terms
Acetylation, Bacterial Proteins, Endoplasmic Reticulum, HeLa Cells, Humans, Lysine, Mitochondria, Models, Molecular, Virulence, Crystallography, X-Ray, SUMO-1 Protein, Virulence Factors

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