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Pectocin M1 (PcaM1) Inhibits Escherichia coli Cell Growth and Peptidoglycan Biosynthesis through Periplasmic Expression
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 homo...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5187517/ https://www.ncbi.nlm.nih.gov/pubmed/27740593 http://dx.doi.org/10.3390/antibiotics5040036 |
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author | Chérier, Dimitri Giacomucci, Sean Patin, Delphine Bouhss, Ahmed Touzé, Thierry Blanot, Didier Mengin-Lecreulx, Dominique Barreteau, Hélène |
author_facet | Chérier, Dimitri Giacomucci, Sean Patin, Delphine Bouhss, Ahmed Touzé, Thierry Blanot, Didier Mengin-Lecreulx, Dominique Barreteau, Hélène |
author_sort | Chérier, Dimitri |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5187517 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-51875172016-12-30 Pectocin M1 (PcaM1) Inhibits Escherichia coli Cell Growth and Peptidoglycan Biosynthesis through Periplasmic Expression Chérier, Dimitri Giacomucci, Sean Patin, Delphine Bouhss, Ahmed Touzé, Thierry Blanot, Didier Mengin-Lecreulx, Dominique Barreteau, Hélène Antibiotics (Basel) Article 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. MDPI 2016-10-08 /pmc/articles/PMC5187517/ /pubmed/27740593 http://dx.doi.org/10.3390/antibiotics5040036 Text en © 2016 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Chérier, Dimitri Giacomucci, Sean Patin, Delphine Bouhss, Ahmed Touzé, Thierry Blanot, Didier Mengin-Lecreulx, Dominique Barreteau, Hélène Pectocin M1 (PcaM1) Inhibits Escherichia coli Cell Growth and Peptidoglycan Biosynthesis through Periplasmic Expression |
title | Pectocin M1 (PcaM1) Inhibits Escherichia coli Cell Growth and Peptidoglycan Biosynthesis through Periplasmic Expression |
title_full | Pectocin M1 (PcaM1) Inhibits Escherichia coli Cell Growth and Peptidoglycan Biosynthesis through Periplasmic Expression |
title_fullStr | Pectocin M1 (PcaM1) Inhibits Escherichia coli Cell Growth and Peptidoglycan Biosynthesis through Periplasmic Expression |
title_full_unstemmed | Pectocin M1 (PcaM1) Inhibits Escherichia coli Cell Growth and Peptidoglycan Biosynthesis through Periplasmic Expression |
title_short | Pectocin M1 (PcaM1) Inhibits Escherichia coli Cell Growth and Peptidoglycan Biosynthesis through Periplasmic Expression |
title_sort | pectocin m1 (pcam1) inhibits escherichia coli cell growth and peptidoglycan biosynthesis through periplasmic expression |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5187517/ https://www.ncbi.nlm.nih.gov/pubmed/27740593 http://dx.doi.org/10.3390/antibiotics5040036 |
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