Proteomic analysis of triclosan resistance in Salmonella enterica serovar Typhimurium

Mark Webber, NG Coldham, MJ Woodward, Laura Piddock

Research output: Contribution to journalArticle

34 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)92-7
Number of pages6
JournalJournal of Antimicrobial Chemotherapy
Early online date1 Apr 2008
Publication statusPublished - 1 Apr 2008


  • biocides
  • proteomics
  • efflux


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