ArticleJournal of bacteriology2013
Structure of microcin B-like compounds produced by Pseudomonas syringae and species specificity of their antibacterial action.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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.
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.
Who cites it
24 citing papers in PubMed, 46 citations in OpenAlex.
- Heterologous expression and functional characterization of novel microcin B17 congeners from environmental Pseudomonas isolates.Applied microbiology and biotechnology · 2026Article
- Friend or Foe: Protein Inhibitors of DNA Gyrase.Biology · 2024Review
- Colicins and Microcins Produced byInternational journal of environmental research and public health · 2022Review
- Microcins reveal natural mechanisms of bacterial manipulation to inform therapeutic development.Microbiology (Reading, England) · 2022Article
- Article
- Pentapeptide repeat protein QnrB1 requires ATP hydrolysis to rejuvenate poisoned gyrase complexes.Nucleic acids research · 2021Article
- Translation-Targeting RiPPs and Where to Find Them.Frontiers in genetics · 2020Review
- Bacteriocins to Thwart Bacterial Resistance in Gram Negative Bacteria.Frontiers in microbiology · 2020Review
- Fic Proteins Inhibit the Activity of Topoisomerase IV by AMPylation in Diverse Bacteria.Frontiers in microbiology · 2020Article
- Structure of ribosome-bound azole-modified peptide phazolicin rationalizes its species-specific mode of bacterial translation inhibition.Nature communications · 2019Article
- The Microbial Toxin Microcin B17: Prospects for the Development of New Antibacterial Agents.Journal of molecular biology · 2019Review
- LlpB represents a second subclass of lectin-like bacteriocins.Microbial biotechnology · 2019Article
- Architecture of Microcin B17 Synthetase: An Octameric Protein Complex Converting a Ribosomally Synthesized Peptide into a DNA Gyrase Poison.Molecular cell · 2019Article
- Single-nucleotide-resolution mapping of DNA gyrase cleavage sites across the Escherichia coli genome.Nucleic acids research · 2019Article
- Heterologous expression and purification of BtCspB, a novel cold-shock protein-like bacteriocin from Bacillus thuringiensis BRC-ZYR2.World journal of microbiology & biotechnology · 2019Article
- Microcins inFrontiers in microbiology · 2019Review
- Lectin-Like Bacteriocins.Frontiers in microbiology · 2018Review
- Heterologous Production of Microbial Ribosomally Synthesized and Post-translationally Modified Peptides.Frontiers in microbiology · 2018Review
- Heterologous Expression of Biopreservative Bacteriocins With a View to Low Cost Production.Frontiers in microbiology · 2018Review
- The Origins of Specificity in the Microcin-Processing Protease TldD/E.Structure (London, England : 1993) · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli microcin B (Ec-McB) is a posttranslationally modified antibacterial peptide containing multiple oxazole and thiazole heterocycles and targeting the DNA gyrase. We have found operons homologous to the Ec-McB biosynthesis-immunity operon mcb in recently sequenced genomes of several pathovars of the plant pathogen Pseudomonas syringae, and we produced two variants of P. syringae microcin B (Ps-McB) in E. coli by heterologous expression. Like Ec-McB, both versions of Ps-McB target the DNA gyrase, but unlike Ec-McB, they are active against various species of the Pseudomonas genus, including human pathogen P. aeruginosa. Through analysis of Ec-McB/Ps-McB chimeras, we demonstrate that three centrally located unmodified amino acids of Ps-McB are sufficient to determine activity against Pseudomonas, likely by allowing specific recognition by a transport system that remains to be identified. The results open the way for construction of McB-based antibacterial molecules with extended spectra of biological activity.
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Registered trials
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.