IMP-27, a Unique Metallo-β-Lactamase Identified in Geographically Distinct Isolates of Proteus mirabilis

• Published in: Antimicrobial agents and chemotherapy Vol. 60; no. 10; pp. 6418 - 6421
• Main Authors: Dixon, Nyssa, Fowler, Randal C, Yoshizumi, A, Horiyama, Tsukasa, Ishii, Y, Harrison, Lucas, Geyer, Chelsie N, Moland, Ellen Smith, Thomson, Kenneth, Hanson, Nancy D
• Format: Journal Article
• Language: English
• Published: United States American Society for Microbiology 01.10.2016
• Subjects: Aztreonam - pharmacology; beta-Lactamases; beta-Lactamases - genetics; beta-Lactamases - metabolism; beta-Lactams - pharmacology; Ceftazidime - pharmacokinetics; Drug Resistance, Bacterial - drug effects; Drug Resistance, Bacterial - genetics; Hydrolysis; Integrons; Mechanisms of Resistance; Microbial Sensitivity Tests; Penicillanic Acid - analogs & derivatives; Penicillanic Acid - pharmacology; Piperacillin - pharmacology; Proteus Infections - microbiology; Proteus mirabilis; Proteus mirabilis - drug effects; Proteus mirabilis - genetics; Proteus mirabilis - isolation & purification; United States
• ISSN: 0066-4804; 1098-6596
• DOI: 10.1128/AAC.02945-15

A novel metallo-β-lactamase gene, blaIMP-27, was identified in unrelated Proteus mirabilis isolates from two geographically distinct locations in the United States. Both isolates harbor blaIMP-27 as part of the first gene cassette in a class 2 integron. Antimicrobial susceptibility testing indicated susceptibility to aztreonam, piperacillin-tazobactam, and ceftazidime but resistance to ertapenem. However, hydrolysis assays indicated that ceftazidime was a substrate for IMP-27.