Evidence map›Paper›PMID 19346308›Full record

ArticleJournal of bacteriology2009

Human- and plant-pathogenic Pseudomonas species produce bacteriocins exhibiting colicin M-like hydrolase activity towards peptidoglycan precursors.

Hélène Barreteau, Ahmed Bouhss, Martine Fourgeaud, Jean-Luc Mainardi, Thierry Touzé, Fabien Gérard, Didier Blanot, Michel Arthur, Dominique Mengin-Lecreulx

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
8.4field-weighted citation impact, top 3% of its field
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

43 citing papers in PubMed, 77 citations in OpenAlex.

  1. Bacteriocins fromFrontiers in microbiology · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Antimicrobial Weapons of Pseudomonas aeruginosa.Advances in experimental medicine and biology · 2022
    Article
  10. The Biology of Colicin M and Its Orthologs.Antibiotics (Basel, Switzerland) · 2021
    Review
  11. Review
  12. LpxT-Dependent Phosphorylation of Lipid A inFrontiers in microbiology · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Lectin-Like Bacteriocins.Frontiers in microbiology · 2018
    Review
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

9 authors at 5 institutions in 1 country.

Hélène BarreteauUniversité Paris-Sud, Institut de Biochimie et Biophysique Moléculaire et Cellulaire, UMR 8619, Orsay F-91405, France.
Ahmed Bouhss
Martine Fourgeaud
Jean-Luc Mainardi
Thierry Touzé
Fabien Gérard
Didier Blanot
Michel Arthur
Dominique Mengin-Lecreulx
Institut de Biochimie et Biophysique Moléculaire et Cellulaire · FRUniversité Paris-Sud · FRCentre de Recherche des Cordeliers · FRDélégation Paris 5 · FRSorbonne Université · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Genes encoding proteins that exhibit similarity to the C-terminal domain of Escherichia coli colicin M were identified in the genomes of some Pseudomonas species, namely, P. aeruginosa, P. syringae, and P. fluorescens. These genes were detected only in a restricted number of strains. In P. aeruginosa, for instance, the colicin M homologue gene was located within the ExoU-containing genomic island A, a large horizontally acquired genetic element and virulence determinant. Here we report the cloning of these genes from the three Pseudomonas species and the purification and biochemical characterization of the different colicin M homologues. All of them were shown to exhibit Mg(2+)-dependent diphosphoric diester hydrolase activity toward the two undecaprenyl phosphate-linked peptidoglycan precursors (lipids I and II) in vitro. In all cases, the site of cleavage was localized between the undecaprenyl and pyrophospho-MurNAc moieties of these precursors. These enzymes were not active on the cytoplasmic precursor UDP-MurNAc-pentapeptide or (or only very poorly) on undecaprenyl pyrophosphate. These colicin M homologues have a narrow range of antibacterial activity. The P. aeruginosa protein at low concentrations was shown to inhibit growth of sensitive P. aeruginosa strains. These proteins thus represent a new class of bacteriocins (pyocins), the first ones reported thus far in the genus Pseudomonas that target peptidoglycan metabolism.

Indexed as

Amino Acid SequenceBacteriocinsChromatography, High Pressure LiquidColicinsHumansMolecular Sequence DataMonosaccharidesOligopeptidesPlantsPseudomonasSequence Homology, Amino AcidSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationUridine Diphosphate N-Acetylmuramic AcidBacteriocinsColicinslipid IMonosaccharidesmuramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenolOligopeptidesUridine Diphosphate N-Acetylmuramic Acid

Identifiers

PMID19346308
PMCPMC2681890
OpenAlexW2166736932

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.