Induction of the Cpx Envelope Stress Pathway Contributes to Escherichia coli Tolerance to Antimicrobial Peptides

Autor: Bianca Audrain, Christophe Beloin, Jean-Yves Coppée, Amira Zairi, Jean-Marc Ghigo, Lionel Ferrières, Curtis B. Dobson, Guillaume Soubigou
Přispěvatelé: Cellule Pasteur, Université Paris Diderot - Paris 7 (UPD7)-PRES Sorbonne Paris Cité, Génétique des Biofilms, Institut Pasteur [Paris] (IP), Faculté de médecine de Sousse [Ibn EL Jazzar], Transcriptome et Epigénome (PF2), Faculty of Life Sciences [Manchester], University of Manchester [Manchester], This work was supported by a grant from the European Commission (grant LSHE-CT-2006-037692) and the French Government's Investissement d'Avenir program Laboratoire d'Excellence 'Integrative Biology of Emerging Infectious Diseases' (grant ANR-10-LABX-62-IBEID)., We thank Sylvie Létoffé for helpful discussions. We also thank Mike Birch, Ai2 Ltd., as well as members of the NPARI consortium for support during the course of this project., ANR-10-LABX-0062,IBEID,Integrative Biology of Emerging Infectious Diseases(2010), European Project: 037692, European STREP 'NPARI', Institut Pasteur [Paris]
Rok vydání: 2013
Předmět:
MESH: Apolipoproteins E/*metabolism
MESH: Signal Transduction
Antimicrobial peptides
Genetics and Molecular Biology
Peptide
Biology
medicine.disease_cause
Applied Microbiology and Biotechnology
Melittin
Microbiology
MESH: Gene Expression Profiling
03 medical and health sciences
chemistry.chemical_compound
Apolipoproteins E
Stress
Physiological

Escherichia coli
medicine
Humans
MESH: Escherichia coli/*drug effects/*physiology
MESH: *Stress
030304 developmental biology
chemistry.chemical_classification
0303 health sciences
MESH: Humans
Dermaseptin
MESH: Anti-Bacterial Agents/*metabolism
Ecology
030306 microbiology
Gene Expression Profiling
Drug Tolerance
Antimicrobial
[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology
Peptide Fragments
Anti-Bacterial Agents
chemistry
MESH: *Drug Tolerance
Signal transduction
Metabolic Networks and Pathways
MESH: Metabolic Networks and Pathways/genetics
Polymyxin B
Signal Transduction
MESH: Peptide Fragments/*metabolism
Food Science
Biotechnology
medicine.drug
Zdroj: Applied and Environmental Microbiology
Applied and Environmental Microbiology, 2013, 79 (24), pp.7770-7779. ⟨10.1128/AEM.02593-13⟩
Applied and Environmental Microbiology, American Society for Microbiology, 2013, 79 (24), pp.7770-7779. ⟨10.1128/AEM.02593-13⟩
ISSN: 1098-5336
0099-2240
Popis: Antimicrobial peptides produced by multicellular organisms as part of their innate system of defense against microorganisms are currently considered potential alternatives to conventional antibiotics in case of infection by multiresistant bacteria. However, while the mode of action of antimicrobial peptides is relatively well described, resistance mechanisms potentially induced or selected by these peptides are still poorly understood. In this work, we studied the mechanisms of action and resistance potentially induced by ApoEdpL-W, a new antimicrobial peptide derived from human apolipoprotein E. Investigation of the genetic response of Escherichia coli upon exposure to sublethal concentrations of ApoEdpL-W revealed that this antimicrobial peptide triggers activation of RcsCDB, CpxAR, and σ E envelope stress pathways. This genetic response is not restricted to ApoEdpL-W, since several other antimicrobial peptides, including polymyxin B, melittin, LL-37, and modified S 4 dermaseptin, also activate several E. coli envelope stress pathways. Finally, we demonstrate that induction of the CpxAR two-component system directly contributes to E. coli tolerance toward ApoEdpL-W, polymyxin B, and melittin. These results therefore show that E. coli senses and responds to different antimicrobial peptides by activation of the CpxAR pathway. While this study further extends the understanding of the array of peptide-induced stress signaling systems, it also provides insight into the contribution of Cpx envelope stress pathway to E. coli tolerance to antimicrobial peptides.
Databáze: OpenAIRE