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Article Dans Une Revue Current Proteomics Année : 2016

Ciprofloxacin stress proteome of the extended-spectrum beta-lactamase producing Escherichia coli from slaughtered pigs

Résumé

The increasing prevalence of bacteria resistant to even the most current arsenal of antibiot- ics is a serious concern for public health globally. The resistant bacteria which cause human infection are thought to emerge in food and animals. Our goal was to study the proteome of an extended- spectrum -lactamase (ESBL)-producing Escherichia coli , SU03, strain recovered from faecal sam- ples of pigs slaughtered for human consumption. This strain exhibited ciprofloxacin resistance asso- ciated 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 overex- pressed when SU03 was cultured with double the minimum inhibitory concentration of ciproflox- acin. Further research should determine how this enzyme contributes to ciprofloxacin resistance.
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Dates et versions

hal-01602438 , version 1 (27-05-2020)

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Sónia Ramos, Ingrid Chafsey, Michel Hébraud, Margarida Sousa, Patrícia Poeta, et al.. Ciprofloxacin stress proteome of the extended-spectrum beta-lactamase producing Escherichia coli from slaughtered pigs. Current Proteomics, 2016, 13, pp.285-289. ⟨10.2174/1570164613666161018144215⟩. ⟨hal-01602438⟩

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