Preprint Review Version 1 Preserved in Portico This version is not peer-reviewed

The Biology of Colicin M and Its Orthologs

Version 1 : Received: 29 July 2021 / Approved: 30 July 2021 / Online: 30 July 2021 (13:27:37 CEST)

A peer-reviewed article of this Preprint also exists.

Chérier, D.; Patin, D.; Blanot, D.; Touzé, T.; Barreteau, H. The Biology of Colicin M and Its Orthologs. Antibiotics 2021, 10, 1109. Chérier, D.; Patin, D.; Blanot, D.; Touzé, T.; Barreteau, H. The Biology of Colicin M and Its Orthologs. Antibiotics 2021, 10, 1109.

Journal reference: Antibiotics 2021, 10, 1109
DOI: 10.3390/antibiotics10091109

Abstract

The misuse of antibiotics during the last decades led to the emergence of multidrug resistant pathogenic bacteria. This phenomenon constitutes a major public health issue. Consequently, the discovery of new antibacterials in the short term is crucial. Colicins, due to their antibacterial properties, thus constitute good candidates. These toxin proteins, produced by E. coli to kill enteric relative competitors, exhibit cytotoxicity through ionophoric activity or essential macromolecule degradation. Among the 25-colicin types known to date, colicin M (ColM) is the only one colicin interfering with peptidoglycan biosynthesis. Accordingly, ColM develops its lethal activity in E. coli periplasm by hydrolyzing the last peptidoglycan precursor, lipid II, into two dead-end products, thereby leading to cell lysis. Since the discovery of its unusual mode of action, several ColM orthologs have also been identified based on sequence alignments; all of the characterized ColM-like proteins display the same enzymatic activity of lipid II degradation and narrow antibacterial spectra. This publication aims at being an exhaustive review about what is currently known on this new family of antibacterial enzymes as well as on their potential use of food preservatives or therapeutic agents.

Keywords

Colicins; colicin M; peptidoglycan; lipid II; antibacterials

Subject

LIFE SCIENCES, Biochemistry

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