Colicins are proteins produced by some strains of Escherichia coli to kill competitors belonging to the same species. Among them, ColM (colicin M) is the only one that blocks the biosynthesis of peptidoglycan, a specific bacterial cell-wall polymer essential for cell integrity. ColM acts in the periplasm by hydrolysing the phosphoester bond of the peptidoglycan lipid intermediate (lipid II). ColM cytotoxicity is dependent on FkpA of the targeted cell, a chaperone with peptidylprolyl cis–trans isomerase activity. Dissection of ColM was used to delineate the catalytic domain and to identify the active-site residues. The in vitro activity of the isolated catalytic domain towards lipid II was 50-fold higher than that of the full-length bacteriocin. Moreover, this domain was bactericidal in the absence of FkpA under conditions that bypass the import mechanism (FhuA–TonB machinery). Thus ColM undergoes a maturation process driven by FkpA that is not required for the activity of the isolated catalytic domain. Genes encoding proteins with similarity to the catalytic domain of ColM were identified in pathogenic strains of Pseudomonas and other genera. ColM acts on several structures of lipid II representative of the diversity of peptidoglycan chemotypes. All together, these data open the way to the potential use of ColM-related bacteriocins as broad spectrum antibacterial agents.
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December 2012
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Conference Article|
November 21 2012
Colicin M, a peptidoglycan lipid-II-degrading enzyme: potential use for antibacterial means?
Thierry Touzé;
Thierry Touzé
1
*Laboratoire des Enveloppes Bactériennes et Antibiotiques, IBBMC, Université Paris-Sud, UMR 8619 CNRS, 91405 Orsay, France
1To whom correspondence should be addressed (emailthierry.touze@u-psud.fr).
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Hélène Barreteau;
Hélène Barreteau
*Laboratoire des Enveloppes Bactériennes et Antibiotiques, IBBMC, Université Paris-Sud, UMR 8619 CNRS, 91405 Orsay, France
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Meriem El Ghachi;
Meriem El Ghachi
2
*Laboratoire des Enveloppes Bactériennes et Antibiotiques, IBBMC, Université Paris-Sud, UMR 8619 CNRS, 91405 Orsay, France
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Ahmed Bouhss;
Ahmed Bouhss
*Laboratoire des Enveloppes Bactériennes et Antibiotiques, IBBMC, Université Paris-Sud, UMR 8619 CNRS, 91405 Orsay, France
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Aurélie Barnéoud-Arnoulet;
Aurélie Barnéoud-Arnoulet
†Laboratoire d’Ingénierie des Systèmes Macromoléculaires, CNRS–Aix Marseille Université, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France
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Delphine Patin;
Delphine Patin
*Laboratoire des Enveloppes Bactériennes et Antibiotiques, IBBMC, Université Paris-Sud, UMR 8619 CNRS, 91405 Orsay, France
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Emmanuelle Sacco;
Emmanuelle Sacco
‡Laboratoire de Recherche Moléculaire sur les Antibiotiques, Centre de Recherche des Cordeliers, Université Pierre et Marie Curie, Université Paris Descartes, INSERM, UMR-S 872, 75006 Paris, France
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Didier Blanot;
Didier Blanot
*Laboratoire des Enveloppes Bactériennes et Antibiotiques, IBBMC, Université Paris-Sud, UMR 8619 CNRS, 91405 Orsay, France
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Michel Arthur;
Michel Arthur
‡Laboratoire de Recherche Moléculaire sur les Antibiotiques, Centre de Recherche des Cordeliers, Université Pierre et Marie Curie, Université Paris Descartes, INSERM, UMR-S 872, 75006 Paris, France
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Denis Duché;
Denis Duché
†Laboratoire d’Ingénierie des Systèmes Macromoléculaires, CNRS–Aix Marseille Université, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France
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Roland Lloubès;
Roland Lloubès
†Laboratoire d’Ingénierie des Systèmes Macromoléculaires, CNRS–Aix Marseille Université, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France
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Dominique Mengin-Lecreulx
Dominique Mengin-Lecreulx
*Laboratoire des Enveloppes Bactériennes et Antibiotiques, IBBMC, Université Paris-Sud, UMR 8619 CNRS, 91405 Orsay, France
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Publisher: Portland Press Ltd
Received:
July 27 2012
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2012 The Authors Journal
2012
Biochem Soc Trans (2012) 40 (6): 1522–1527.
Article history
Received:
July 27 2012
Citation
Thierry Touzé, Hélène Barreteau, Meriem El Ghachi, Ahmed Bouhss, Aurélie Barnéoud-Arnoulet, Delphine Patin, Emmanuelle Sacco, Didier Blanot, Michel Arthur, Denis Duché, Roland Lloubès, Dominique Mengin-Lecreulx; Colicin M, a peptidoglycan lipid-II-degrading enzyme: potential use for antibacterial means?. Biochem Soc Trans 1 December 2012; 40 (6): 1522–1527. doi: https://doi.org/10.1042/BST20120189
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