Protein aggregation is a consequence of the dormancy-inducing membrane toxin TisB in <i>Escherichia coli</i>

Protein aggregates occur in all living cells due to misfolding of proteins. In bacteria, protein aggregation is associated with cellular inactivity, which is related to dormancy and tolerance to stressful conditions, including exposure to antibiotics. In <i>Escherichia coli</i>, the membrane toxin TisB is an important factor for dormancy and antibiotic tolerance upon DNA damage mediated by the fluoroquinolone antibiotic ciprofloxacin. Here, we show that TisB provokes protein aggregation, which, in turn, promotes an extended state of cellular dormancy. Our study suggests that protein aggregation is a consequence of membrane toxins with the potential to affect the duration of dormancy and the outcome of antibiotic therapy.

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Publication Details

Journal
mSystems
Published
2024-10-08
DOI
https://doi.org/10.1128/msystems.01060-24
Citations
8
Primary Topic
Bacterial Genetics and Biotechnology
Type
article
Field-Weighted Citation Impact
4.40

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article

Protein aggregation is a consequence of the dormancy-inducing membrane toxin TisB in Escherichia coli

Sebastian Schmidt, Maximilian H. Ulbrich, Ana Natriashvili, Florian H. Leinberger et al.
8 citations
mSystems
Bacterial Genetics and Biotechnology
4.40
article

Protein aggregation is a consequence of the dormancy-inducing membrane toxin TisB in Escherichia coli

Sebastian Schmidt, Maximilian H. Ulbrich, Ana Natriashvili, Florian H. Leinberger, Daniel Edelmann, Andreas Tholey, Patrick Blumenkamp, Nicole E. Schmid, Hans‐Georg Koch, Markus Oberpaul, Bork A. Berghoff, Liam Cassidy
article en
8 citations

Abstract

Protein aggregates occur in all living cells due to misfolding of proteins. In bacteria, protein aggregation is associated with cellular inactivity, which is related to dormancy and tolerance to stressful conditions, including exposure to antibiotics. In <i>Escherichia coli</i>, the membrane toxin TisB is an important factor for dormancy and antibiotic tolerance upon DNA damage mediated by the fluoroquinolone antibiotic ciprofloxacin. Here, we show that TisB provokes protein aggregation, which, in turn, promotes an extended state of cellular dormancy. Our study suggests that protein aggregation is a consequence of membrane toxins with the potential to affect the duration of dormancy and the outcome of antibiotic therapy.

mSystemsVol. 9(11)
University of Freiburg (DE), Justus-Liebig-Universität Gießen (DE), Christian-Albrechts-Universität zu Kiel (DE), Fraunhofer Institute for Molecular Biology and Applied Ecology (DE), Proteome Sciences (United Kingdom) (GB)
Fonds der Chemischen Industrie, Deutsche Forschungsgemeinschaft
Responsible consumption and production
Openalex Percentile: Top 5%
Bacterial Genetics and Biotechnology
4.40
DOIOpen Access PDFOpenAlex
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Protein aggregation is a consequence of the dormancy-inducing membrane toxin TisB in <i>Escherichia coli</i> — Sebastian Schmidt, Maximilian H. Ulbrich, et al. · mSystems (2024) | TGRS Research Map | TGRS