Genetic and biochemical characterization of the chromosome-encoded class B β-lactamases from Shewanella livingstonensis (SLB-1) and Shewanella frigidimarina (SFB-1)

Objectives: To determine the β-lactamase gene content of β-lactam-susceptible psychrophilic Gram-negative bacilli, Shewanella frigidimarina and Shewanella livingstonensis, isolated from a marine environment. Methods: β-Lactamase genes were cloned, sequenced and expressed in Escherichia coli. Kinetic...

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Bibliographic Details
Published in:Journal of antimicrobial chemotherapy 2005-05, Vol.55 (5), p.680-685
Main Authors: Poirel, Laurent, Héritier, Claire, Nordmann, Patrice
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Antibiotics. Antiinfectious agents. Antiparasitic agents
beta-Lactam Resistance
beta-Lactamases - genetics
beta-Lactamases - metabolism
beta-Lactams - pharmacology
Biological and medical sciences
carbapenems
Chromosomes, Bacterial - genetics
Cloning, Molecular
Escherichia coli
Medical sciences
metallo-β-lactamases
Microbial Sensitivity Tests
Molecular Sequence Data
Pharmacology. Drug treatments
Pseudomonas aeruginosa
S. frigidimarina
S. livingstonensis
Sequence Analysis, DNA
Shewanella - classification
Shewanella - drug effects
Shewanella - enzymology
Shewanella - genetics
Shewanella frigidimarina
Shewanella livingstonensis
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Summary:Objectives: To determine the β-lactamase gene content of β-lactam-susceptible psychrophilic Gram-negative bacilli, Shewanella frigidimarina and Shewanella livingstonensis, isolated from a marine environment. Methods: β-Lactamase genes were cloned, sequenced and expressed in Escherichia coli. Kinetic parameters were determined using purified enzymes. Results: Metallo-β-lactamases SLB-1 and SFB-1 were identified from S. livingstonensis and S. frigidimarina, respectively, sharing 65% amino acid identity and being distantly related to other Ambler class B β-lactamases (40 and 36% amino acid identity with GIM-1 and IMP-1 from Pseudomonas aeruginosa, respectively). SLB-1 had an EDTA-inhibited and broad-spectrum β-lactam hydrolysis profile, whereas SFB-1 did not hydrolyse cephalosporins, with activity being weakly inhibited by EDTA and dipicolinic acid. Conclusions: This work provides further evidence that psychrophilic bacterial species may constitute a reservoir of β-lactam resistance genes.
ISSN:0305-7453
1460-2091
DOI:10.1093/jac/dki065