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

Antimicrob Agents Chemother. 2016 Sep 23;60(10):6418-21. doi: 10.1128/AAC.02945-15. Print 2016 Oct.

Abstract

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.

MeSH terms

  • Aztreonam / pharmacology
  • Ceftazidime / pharmacokinetics
  • Drug Resistance, Bacterial / drug effects
  • Drug Resistance, Bacterial / genetics
  • Ertapenem
  • Hydrolysis
  • Integrons
  • Microbial Sensitivity Tests
  • Penicillanic Acid / analogs & derivatives
  • Penicillanic Acid / pharmacology
  • Piperacillin / pharmacology
  • Piperacillin, Tazobactam Drug Combination
  • Proteus Infections / microbiology
  • Proteus mirabilis / drug effects*
  • Proteus mirabilis / genetics*
  • Proteus mirabilis / isolation & purification
  • United States
  • beta-Lactamases / genetics*
  • beta-Lactamases / metabolism
  • beta-Lactams / pharmacology

Substances

  • beta-Lactams
  • Piperacillin, Tazobactam Drug Combination
  • Penicillanic Acid
  • Ceftazidime
  • beta-Lactamases
  • Aztreonam
  • Ertapenem
  • Piperacillin

Grants and funding

Funding for this project was provided by Streck, Inc., and Shionogi & Co., Ltd. T. Horiyama is an employee of Shionogi & Co., Ltd. N. D. Hanson has funding from Streck, Inc. The remaining authors declare no conflicts of interest. The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.