Characterization of colicin M and its orthologs targeting bacterial cell wall peptidoglycan biosynthesis. - Archive ouverte HAL Access content directly
Journal Articles Microb. Drug Resist. Year : 2012

Characterization of colicin M and its orthologs targeting bacterial cell wall peptidoglycan biosynthesis.

Abstract

For a long time, colicin M was known for killing susceptible Escherichia coli cells by interfering with cell wall peptidoglycan biosynthesis, but its precise mode of action was only recently elucidated: this bacterial toxin was demonstrated to be an enzyme that catalyzes the specific degradation of peptidoglycan lipid intermediate II, thereby provoking the arrest of peptidoglycan synthesis and cell lysis. The discovery of this activity renewed the interest in this colicin and opened the way for biochemical and structural analyses of this new class of enzyme (phosphoesterase). The identification of a few orthologs produced by pathogenic strains of Pseudomonas further enlarged the field of investigation. The present article aims at reviewing recently acquired knowledge on the biology of this small family of bacteriocins.

Dates and versions

hal-01458251 , version 1 (06-02-2017)

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Hélène Barreteau, Meriem El Ghachi, Aurélie Barnéoud-Arnoulet, Emmanuelle Sacco, Thierry Touzé, et al.. Characterization of colicin M and its orthologs targeting bacterial cell wall peptidoglycan biosynthesis.. Microb. Drug Resist., 2012, 18 (3), pp.222--9. ⟨10.1089/mdr.2011.0230⟩. ⟨hal-01458251⟩
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