Colicin M, a peptidoglycan lipid-II-degrading enzyme: potential use for antibacterial means?

Abstract:

: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.

journal_name

Biochem Soc Trans

authors

Touzé T,Barreteau H,El Ghachi M,Bouhss A,Barnéoud-Arnoulet A,Patin D,Sacco E,Blanot D,Arthur M,Duché D,Lloubès R,Mengin-Lecreulx D

doi

10.1042/BST20120189

subject

Has Abstract

pub_date

2012-12-01 00:00:00

pages

1522-7

issue

6

eissn

0300-5127

issn

1470-8752

pii

BST20120189

journal_volume

40

pub_type

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