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

Nyssa Dixon; Randal C Fowler; A Yoshizumi; Tsukasa Horiyama; Y Ishii; Lucas Harrison; Chelsie N Geyer; Ellen Smith Moland; Kenneth Thomson; Nancy D Hanson

doi:10.1128/AAC.02945-15

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.

Authors

Affiliations

¹ Creighton University School of Medicine, Department of Medical Microbiology and Immunology, Center for Research in Anti-Infectives and Biotechnology, Omaha, Nebraska, USA.
² Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska, USA.
³ School of Medical Technology, Gumma Paz College, Takasakishi, Gumma, Japan.
⁴ Shionogi & Co., Ltd., Osaka, Japan.
⁵ Toho University School of Medicine, Department of Microbiology and Infectious Diseases, Tokyo, Japan.
⁶ CHI Health, Omaha, Nebraska, USA.
⁷ University of Louisville School of Medicine, Louisville, Kentucky, USA.
⁸ Creighton University School of Medicine, Department of Medical Microbiology and Immunology, Center for Research in Anti-Infectives and Biotechnology, Omaha, Nebraska, USA [email protected].

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.