Biochemical Characterization of CPS-1, a Subclass B3 Metallo-β-Lactamase from a Chryseobacterium piscium Soil Isolate.

Dereje Dadi Gudeta, Simona Pollini, Jean-Denis Docquier, Valeria Bortolaia, Gian Maria Rossolini, Luca Guardabassi

Journal: Antimicrobial agents and chemotherapy 2016;60(3):1869-73

PMID: 26666948

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Abstract

CPS-1 is a subclass B3 metallo-β-lactamase from a Chryseobacterium piscium isolate collected from soil, showing 68% amino acid identity to the GOB-1 enzyme. CPS-1 was overproduced in Escherichia coli Rosetta (DE3), purified by chromatography, and biochemically characterized. This enzyme exhibits a broad-spectrum substrate profile, including penicillins, cephalosporins, and carbapenems, which overall resembles those of L1, GOB-1, and acquired subclass B3 enzymes AIM-1 and SMB-1.

Address: Department of Veterinary Disease Biology, Faculty of Health and Medical Sciences, University of Copenhagen, Frederiksberg, Denmark.; Department of Medical Biotechnologies, University of Siena, Siena, Italy.; Department of Medical Biotechnologies, University of Siena, Siena, Italy Department of Experimental and Clinical Medicine, University of Florence, Florence, Italy Clinical Microbiology and Virology Unit, Florence Careggi University Hospital, Florence, Italy.; Department of Veterinary Disease Biology, Faculty of Health and Medical Sciences, University of Copenhagen, Frederiksberg, Denmark Department of Biomedical Sciences, Ross University School of Veterinary Medicine, St. Kitts, West Indies [email protected].

DOI: 10.1128/AAC.01924-15