JAC Advance Access originally published online on April 3, 2008
Journal of Antimicrobial Chemotherapy 2008 62(1):92-97; doi:10.1093/jac/dkn138
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Original research |
Proteomic analysis of triclosan resistance in Salmonella enterica serovar Typhimurium
1 Antimicrobial Agents Research Group, Division of Immunity and Infection, The University of Birmingham, Edgbaston, Birmingham B15 2TT, UK 2 Veterinary Laboratories Agency (Weybridge), New Haw, Addlestone, Surrey KT15 3NB, UK
Received 14 January 2008; returned 12 February 2008; revised 6 March 2008; accepted 9 March 2008
* Corresponding author. Tel: +44-121-414-2859; Fax: +44-121-414-6815; E-mail: m.a.webber{at}bham.ac.uk
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.
Keywords: biocides , efflux , proteomics