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

Proteomic analysis of triclosan resistance in Salmonella enterica serovar Typhimurium.

Author information

1
Antimicrobial Agents Research Group, Division of Immunity and Infection, The University of Birmingham, Edgbaston, Birmingham B152TT, UK. m.a.webber@bham.ac.uk

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.

PMID:
18388111
DOI:
10.1093/jac/dkn138
[Indexed for MEDLINE]

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