ArticlePLoS genetics2017
CbtA toxin of Escherichia coli inhibits cell division and cell elongation via direct and independent interactions with FtsZ and MreB.
Article in PLoS genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 52 citations in OpenAlex.
- Phylogenomic framework and virulence gene boundaries of emerging Shiga toxin-producingVirulence · 2026Article
- Genomic profiling ofMicrobiology spectrum · 2026Article
- Bacterial defense systems: Mechanisms, homology to eukaryotic immune systems, and applications.Zoological research · 2026Review
- KilR ofmSphere · 2025Article
- YprA family helicases provide the missing link between diverse prokaryotic immune systems.bioRxiv : the preprint server for biology · 2025Article
- MreB: unraveling the molecular mechanisms of bacterial shape, division, and environmental adaptation.Cell communication and signaling : CCS · 2025Review
- The Trade-Off Between Sanitizer Resistance and Virulence Genes: Genomic Insights intoAntibiotics (Basel, Switzerland) · 2025Article
- A Predicted Helix-Turn-Helix Core Is Critical for Bacteriophage Kil Peptide to DisruptAntibiotics (Basel, Switzerland) · 2025Article
- Type I toxin-antitoxin systems in bacteria: from regulation to biological functions.EcoSal Plus · 2024Review
- Unraveling the evolutionary dynamics of toxin-antitoxin systems in diverse genetic lineages ofmBio · 2024Article
- Focused Overview ofBiomimetics (Basel, Switzerland) · 2023Review
- The structural basis of hyperpromiscuity in a core combinatorial network of type II toxin-antitoxin and related phage defense systems.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Bacterial toxin-antitoxin modules: classification, functions, and association with persistence.Current research in microbial sciences · 2021Review
- A newly identified prophage-encoded gene,Journal of bacteriology · 2021Article
- Optimization of a bacterial three-hybrid assay through in vivo titration of an RNA-DNA adapter protein.RNA (New York, N.Y.) · 2021Article
- Modeling the MreB-CbtA Interaction to Facilitate the Prediction and Design of Candidate Antibacterial Peptides.Frontiers in molecular biosciences · 2021Article
- Synergistic Antibacterial and Antibiofilm Activity of the MreB Inhibitor A22 Hydrochloride in Combination with Conventional Antibiotics againstInternational journal of microbiology · 2021Article
- A peptide of a type I toxin-antitoxin system inducesProceedings of the National Academy of Sciences of the United States of America · 2020Article
- AimB Is a Small Protein Regulator of Cell Size and MreB Assembly.Biophysical journal · 2020Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The toxin components of toxin-antitoxin modules, found in bacterial plasmids, phages, and chromosomes, typically target a single macromolecule to interfere with an essential cellular process. An apparent exception is the chromosomally encoded toxin component of the E. coli CbtA/CbeA toxin-antitoxin module, which can inhibit both cell division and cell elongation. A small protein of only 124 amino acids, CbtA, was previously proposed to interact with both FtsZ, a tubulin homolog that is essential for cell division, and MreB, an actin homolog that is essential for cell elongation. However, whether or not the toxic effects of CbtA are due to direct interactions with these predicted targets is not known. Here, we genetically separate the effects of CbtA on cell elongation and cell division, showing that CbtA interacts directly and independently with FtsZ and MreB. Using complementary genetic approaches, we identify the functionally relevant target surfaces on FtsZ and MreB, revealing that in both cases, CbtA binds to surfaces involved in essential cytoskeletal filament architecture. We show further that each interaction contributes independently to CbtA-mediated toxicity and that disruption of both interactions is required to alleviate the observed toxicity. Although several other protein modulators are known to target FtsZ, the CbtA-interacting surface we identify represents a novel inhibitory target. Our findings establish CbtA as a dual function toxin that inhibits both cell division and cell elongation via direct and independent interactions with FtsZ and MreB.
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