Next Article in Journal
Antimicrobial Usage and Antimicrobial Resistance in Animal Production in Southeast Asia: A Review
Next Article in Special Issue
Bulgecin A: The Key to a Broad‐Spectrum Inhibitor That Targets Lytic Transglycosylases
Previous Article in Journal / Special Issue
Resistance to β-Lactams in Neisseria ssp Due to Chromosomally Encoded Penicillin-Binding Proteins
Article Menu

Export Article

Open AccessArticle
Antibiotics 2016, 5(4), 36;

Pectocin M1 (PcaM1) Inhibits Escherichia coli Cell Growth and Peptidoglycan Biosynthesis through Periplasmic Expression

Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette 91198, France
Present address: Department of Microbiology, Infectiology and Immunology, Université de Montréal, Montréal, QC H3T 1J4, Canada.
Present address: Laboratoire Structure-Activité des Biomolécules Normales et Pathologiques, INSERM UMRS 1204 and Université Evry-Val d’Essonne, Evry 91025, France.
Author to whom correspondence should be addressed.
Academic Editor: Christopher Butler
Received: 18 July 2016 / Revised: 14 September 2016 / Accepted: 23 September 2016 / Published: 8 October 2016
(This article belongs to the Special Issue Bacterial Cell Wall as Antimicrobial Target)
Full-Text   |   PDF [2535 KB, uploaded 8 October 2016]   |  


Colicins are bacterial toxins produced by some Escherichia coli strains. They exhibit either enzymatic or pore-forming activity towards a very limited number of bacterial species, due to the high specificity of their reception and translocation systems. Yet, we succeeded in making the colicin M homologue from Pectobacterium carotovorum, pectocin M1 (PcaM1), capable of inhibiting E. coli cell growth by bypassing these reception and translocation steps. This goal was achieved through periplasmic expression of this pectocin. Indeed, when appropriately addressed to the periplasm of E. coli, this pectocin could exert its deleterious effects, i.e., the enzymatic degradation of the peptidoglycan lipid II precursor, which resulted in the arrest of the biosynthesis of this essential cell wall polymer, dramatic morphological changes and, ultimately, cell lysis. This result leads to the conclusion that colicin M and its various orthologues constitute powerful antibacterial molecules able to kill any kind of bacterium, once they can reach their lipid II target. They thus have to be seriously considered as promising alternatives to antibiotics. View Full-Text
Keywords: pectocin M1; peptidoglycan; bacteriocin; colicin; periplasmic expression pectocin M1; peptidoglycan; bacteriocin; colicin; periplasmic expression

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material


Share & Cite This Article

MDPI and ACS Style

Chérier, D.; Giacomucci, S.; Patin, D.; Bouhss, A.; Touzé, T.; Blanot, D.; Mengin-Lecreulx, D.; Barreteau, H. Pectocin M1 (PcaM1) Inhibits Escherichia coli Cell Growth and Peptidoglycan Biosynthesis through Periplasmic Expression. Antibiotics 2016, 5, 36.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Antibiotics EISSN 2079-6382 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top