Proteomic analysis of triclosan resistance in Salmonella enterica serovar Typhimurium

J Antimicrob Chemother. 2008 Jul;62(1):92-7. doi: 10.1093/jac/dkn138. Epub 2008 Apr 3.

Abstract

Objectives: The aim of this study was to determine and compare the proteomes of three triclosan-resistant mutants of Salmonella enterica serovar Typhimurium in order to identify proteins involved in triclosan resistance.

Methods: The proteomes of three distinct but isogenic triclosan-resistant mutants were determined using two-dimensional liquid chromatography mass separation. Bioinformatics was then used to identify and quantify tryptic peptides in order to determine protein expression.

Results: Proteomic analysis of the triclosan-resistant mutants identified a common set of proteins involved in production of pyruvate or fatty acid with differential expression in all mutants, but also demonstrated specific patterns of expression associated with each phenotype.

Conclusions: These data show that triclosan resistance can occur via distinct pathways in Salmonella, and demonstrate a novel triclosan resistance network that is likely to have relevance to other pathogenic bacteria subject to triclosan exposure and may provide new targets for development of antimicrobial agents.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / isolation & purification*
  • Chromatography, Liquid
  • Drug Resistance, Bacterial*
  • Electrophoresis, Gel, Two-Dimensional
  • Gene Expression Profiling
  • Mass Spectrometry
  • Proteome / analysis*
  • Salmonella typhimurium / chemistry
  • Salmonella typhimurium / drug effects*
  • Triclosan / pharmacology*

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Proteome
  • Triclosan