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

doi:10.1128/AAC.01924-15

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

Research output: Contribution to journal › Journal article › Research › peer-review

13 Citations (Scopus)

Abstract

CPS-1 is a subclass B3 metallo-β-lactamase from a Chryseobacterium piscium isolated from soil, showing 68 % amino acid identity to 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.

Original language	English
Journal	Antimicrobial Agents and Chemotherapy
Volume	60
Issue number	3
Pages (from-to)	1869-1873
ISSN	0066-4804
DOIs	https://doi.org/10.1128/AAC.01924-15
Publication status	Published - Mar 2016

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10.1128/AAC.01924-15

Cite this

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

abstract = "CPS-1 is a subclass B3 metallo-β-lactamase from a Chryseobacterium piscium isolated from soil, showing 68 % amino acid identity to 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.",

author = "Gudeta, {Dereje Dadi} and Simona Pollini and Jean-Denis Docquier and Valeria Bortolaia and Rossolini, {Gian Maria} and Luca Guardabassi",

year = "2016",

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doi = "10.1128/AAC.01924-15",

language = "English",

volume = "60",

pages = "1869--1873",

journal = "Antimicrobial Agents and Chemotherapy",

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publisher = "American Society for Microbiology",

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T1 - Biochemical Characterization of CPS-1, a Subclass B3 Metallo-β-Lactamase from a Chryseobacterium piscium Soil Isolate

AU - Gudeta, Dereje Dadi

AU - Pollini, Simona

AU - Docquier, Jean-Denis

AU - Bortolaia, Valeria

AU - Rossolini, Gian Maria

AU - Guardabassi, Luca

PY - 2016/3

Y1 - 2016/3

N2 - CPS-1 is a subclass B3 metallo-β-lactamase from a Chryseobacterium piscium isolated from soil, showing 68 % amino acid identity to 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.

AB - CPS-1 is a subclass B3 metallo-β-lactamase from a Chryseobacterium piscium isolated from soil, showing 68 % amino acid identity to 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.

U2 - 10.1128/AAC.01924-15

DO - 10.1128/AAC.01924-15

M3 - Journal article

C2 - 26666948

SN - 0066-4804

VL - 60

SP - 1869

EP - 1873

JO - Antimicrobial Agents and Chemotherapy

JF - Antimicrobial Agents and Chemotherapy

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