4.7 Article

Proteomic analysis of triclosan resistance in Salmonella enterica serovar Typhimurium

Journal

JOURNAL OF ANTIMICROBIAL CHEMOTHERAPY
Volume 62, Issue 1, Pages 92-97

Publisher

OXFORD UNIV PRESS
DOI: 10.1093/jac/dkn138

Keywords

biocides; efflux; proteomics

Funding

  1. Biotechnology and Biological Sciences Research Council [BB/D020476/1] Funding Source: Medline
  2. Biotechnology and Biological Sciences Research Council [BB/D020476/1] Funding Source: researchfish
  3. BBSRC [BB/D020476/1] Funding Source: UKRI

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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.

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