Proteomic analysis of arsenite - mediated multiple antibiotic resistance in Yersinia enterocolitica biovar 1A

Arsenic is one of the most important global environmental pollutants. In the present study, fifty one clinical strains of Yersinia enterocolitica biovar 1A showed high resistance to arsenite and arsenate. The minimum inhibitory concentration (MIC) of arsenite (0.625–20 mM) was lower than arsenate (1...

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Bibliographic Details
Published in:Journal of basic microbiology 2012-06, Vol.52 (3), p.306-313
Main Authors: Mallik, Sarita, Virdi, Jugsharan Singh, Johri, Atul Kumar
Format: Article
Language:English
Subjects:
Anti-Bacterial Agents - pharmacology
Arsenates - toxicity
Arsenic resistance
Arsenites - toxicity
Bacterial Proteins - analysis
Drug Resistance, Bacterial
Gene Expression Profiling
MALDI-TOF/MS
Microbial Sensitivity Tests
Multiple antibiotic resistance
Proteome - analysis
Stress, Physiological
Yersinia enterocolitica
Yersinia enterocolitica - chemistry
Yersinia enterocolitica - drug effects
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Summary:Arsenic is one of the most important global environmental pollutants. In the present study, fifty one clinical strains of Yersinia enterocolitica biovar 1A showed high resistance to arsenite and arsenate. The minimum inhibitory concentration (MIC) of arsenite (0.625–20 mM) was lower than arsenate (10–80 mM). Growth of Y. enterocolitica in 2 mM arsenite led to 2–8 fold increase in MICs of the five antibiotics (amikacin, ciprofloxacin, gentamycin, kanamycin and tetracycline), suggesting expression of arsenite‐induced multiple antibiotic resistance among the strains. Proteomic analysis of Y. enterocolitica revealed differential expression of certain proteins following arsenite exposure, which included a putative outer membrane porin (OmpA) and a putative amino acid transporter protein. In conclusion, modulation of membrane permeability may be involved in the induction of arsenite–mediated expression of multiple antibiotic resistance in Y. enterocolitica. (© 2012 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)
ISSN:0233-111X
1521-4028
DOI:10.1002/jobm.201100109