Ciprofloxacin Stress Proteome of the Extended-Spectrum β-lactamase Producing Escherichia coli from Slaughtered Pigs

Author(s): Sonia Ramos, Ingrid Chafsey, Michel Hebraud, Margarida Sousa, Patricia Poeta, Gilberto Igrejas

Journal Name: Current Proteomics

Volume 13 , Issue 4 , 2016

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Graphical Abstract:


Background: Escherichia coli with its large range of pathologies is a major cause of human morbidity and mortality around the world. The increasing prevalence of bacteria resistant to even the most current arsenal of antibiotics is a serious concern for public health globally. The resistant bacteria which cause human infection are thought to emerge in food and animals.

Objective: Our goal was to study the proteome of an extended-spectrum β-lactamase (ESBL)- producing Escherichia coli, SU03, strain recovered from faecal samples of pigs slaughtered for human consumption.

Method: A full proteomic survey of this strain was made by two-dimensional electrophoresis identifying proteins by MALDI-TOF/MS.

Results: This strain exhibited ciprofloxacin resistance associated with mutations in type II topoisomerase structural gene GyrA (Ser83Leu + Asp87Asn) and ParC (Ser80Ile). We studied how the proteome of this strain responded to stress by applying double the minimum inhibitory concentration of ciprofloxacin. The hydrolase L-asparaginase was overexpressed when SU03 was cultured with double the minimum inhibitory concentration of ciprofloxacin.

Conclusion: The abundance of this hydrolase may lead to a diverse secondary response by influencing in the production of other proteins or directly mediating ciprofloxacin resistance. Further research should determine how this enzyme contributes to ciprofloxacin resistance.

Keywords: Antibiotic resistance, ciprofloxacin, ESBL, Escherichia coli, proteomics.

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Article Details

Year: 2016
Page: [285 - 289]
Pages: 5
DOI: 10.2174/1570164613666161018144215
Price: $25

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