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• W2115240116 abstract "Limited β-lactams show antipseudomonal activity. The rapid spread of IMP-type metallo-β-lactamases (MBLs), which have a broad spectrum of substrates and a poor susceptibility to clinically available inhibitors, further restricts β-lactam use. In the present study, we evaluated the potency of IMP-10 MBL in hydrolysing antipseudomonal β-lactams currently available in the clinic. Crude IMP-10 MBL was prepared from two clinical isolates of Pseudomonas aeruginosa harbouring the bla IMP-10 gene. The sensitivity of β-lactams to hydrolysis by IMP-10 MBL was determined by comparing the MICs of 14 antipseudomonal β-lactams against a susceptible strain of P. aeruginosa in the presence and absence of IMP-10 MBL. Carbapenems (imipenem, meropenem and panipenem) and extended-spectrum cephems (ceftazidime, cefoperazone, cefsulodin and cefepime) were sensitive to the hydrolysing activity of IMP-10 MBL. By comparison, the fourth-generation cephem (cefpirome), the extended-spectrum penicillins (carbenicillin, ticarcillin, piperacillin and mezlocillin) and monobactams (aztreonam and carumonam) were relatively resistant to IMP-10 MBL. The sensitivity profile of antipseudomonal β-lactams to IMP-10 MBL generated in the present study provides a valuable reference for antibiotic selection by medical professionals." @default.
• W2115240116 created "2016-06-24" @default.
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• W2115240116 date "2008-08-01" @default.
• W2115240116 modified "2023-10-18" @default.
• W2115240116 title "Potency of IMP-10 metallo-β-lactamase in hydrolysing various antipseudomonal β-lactams" @default.
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• W2115240116 doi "https://doi.org/10.1099/jmm.0.2008/001388-0" @default.
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