A novel β-lactamase CTX-M-190, derived from CTX-M-55 by a single substitution Ser133Thr, was identified in a natural Escherichia coli clinical isolate. CTX-M-190 exhibited potent hydrolytic activity against cefotaxime with kcat/Km 14.5 μM-1 s-1 and was resistant to inhibition by β-lactamase inhibitors tazobactam and sulbactam with the 50% inhibitory concentrations 77- and 55-fold higher than those of CTX-M-55, respectively. blaCTX-M-190 was located within the genetic platform, ISEcp1-blaCTX-M-orf477, which was harbored by a 70kb IncI1 plasmid.
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