Regulation of Salmonella typhimurium virulence gene expression by cationic antimicrobial peptides
- 20 August 2003
- journal article
- website
- Published by Wiley in Molecular Microbiology
- Vol. 50 (1) , 219-230
- https://doi.org/10.1046/j.1365-2958.2003.03675.x
Abstract
Summary: Cationic antimicrobial peptides (CAMP) represent a conserved and highly effective component of innate immunity. During infection, the Gram‐negative pathogen Salmonella typhimurium induces different mechanisms of CAMP resistance that promote pathogenesis in animals. This study shows that exposure of S. typhimurium to sublethal concentrations of CAMP activates the PhoP/PhoQ and RpoS virulence regulons, while repressing the transcription of genes required for flagella synthesis and the invasion‐associated type III secretion system. We further demonstrate that growth of S. typhimurium in low doses of the α‐helical peptide C18G induces resistance to CAMP of different structural classes. Inducible resistance depends on the presence of PhoP, indicating that the PhoP/PhoQ system can sense sublethal concentrations of cationic antimicrobial peptides. Growth of S. typhimurium in the presence of CAMP also leads to RpoS‐dependent protection against hydrogen peroxide. Because bacterial resistance to oxidative stress and CAMP are induced during infection of animals, CAMP may be an important signal recognized by bacteria on colonization of animal tissues.Keywords
This publication has 104 references indexed in Scilit:
- Structure of the Cathelicidin Motif of Protegrin-3 Precursor: Structural Insights into the Activation Mechanism of an Antimicrobial ProteinStructure, 2002
- A NEWAPPROACH TODECODINGLIFE: Systems BiologyAnnual Review of Genomics and Human Genetics, 2001
- Stages of Polymyxin B Interaction with the Escherichia coli Cell EnvelopeAntimicrobial Agents and Chemotherapy, 2000
- Cationic peptides: a new source of antibioticsTrends in Biotechnology, 1998
- Signal Detection by the PhoQ Sensor-TransmitterJournal of Biological Chemistry, 1996
- Protegrins: leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesinsFEBS Letters, 1993
- Defensins: Antimicrobial and Cytotoxic Peptides of Mammalian CellsAnnual Review of Immunology, 1993
- Interactions between magainin 2 and Salmonella typhimurium outer membranes: effect of lipopolysaccharide structureBiochemistry, 1991
- Crystal Structure of Defensin HNP-3, an Amphiphilic Dimer: Mechanisms of Membrane PermeabilizationScience, 1991
- Outer membrane of Salmonella typhimurium: accessibility of phospholipid head groups to phospholipase C and cyanogen bromide activated dextran in the external mediumBiochemistry, 1976