Biochemical Characterization of VIM-39, a VIM-1-Like Metallo-β-Lactamase Variant from a Multidrug-Resistant Klebsiella pneumoniae Isolate from Greece

VIM-39, a VIM-1-like metallo-β-lactamase variant (VIM-1 Thr33Ala His224Leu) was identified in a clinical isolate of Klebsiella pneumoniae belonging to sequence type 147. VIM-39 hydrolyzed ampicillin, cephalothin, and imipenem more efficiently than did VIM-1 and VIM-26 (a VIM-1 variant with the His22...

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Bibliographic Details
Published in:Antimicrobial agents and chemotherapy 2015-12, Vol.59 (12), p.7811-7814
Main Authors: Papagiannitsis, Costas C, Pollini, Simona, De Luca, Filomena, Rossolini, Gian Maria, Docquier, Jean-Denis, Hrabák, Jaroslav
Format: Article
Language:English
Subjects:
Ampicillin
Ampicillin - metabolism
Ampicillin - pharmacology
Anti-Bacterial Agents
Anti-Bacterial Agents - metabolism
Anti-Bacterial Agents - pharmacology
Bacterial Typing Techniques
Base Sequence
beta-Lactam Resistance - genetics
beta-Lactamases - genetics
beta-Lactamases - metabolism
Biochemistry, biophysics & molecular biology
Biochimie, biophysique & biologie moléculaire
Biotransformation
Cephalothin
Cephalothin - metabolism
Cephalothin - pharmacology
DNA sequence
Escherichia coli
Gene Expression
Greece
Humans
Hydrolysis
Imipenem
Imipenem - metabolism
Imipenem - pharmacology
Isoenzymes
Isoenzymes - genetics
Isoenzymes - metabolism
Kinetics
Klebsiella Infections
Klebsiella Infections - drug therapy
Klebsiella Infections - microbiology
Klebsiella pneumoniae
Klebsiella pneumoniae - drug effects
Klebsiella pneumoniae - enzymology
Klebsiella pneumoniae - genetics
Klebsiella pneumoniae - isolation & purification
Life sciences
Mechanisms of Resistance
Microbial Sensitivity Tests
Microbiologie
Microbiology
Molecular Sequence Data
Sciences du vivant
Sequence Analysis, DNA
VIM-1 metallo-beta-lactamase
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Description
Summary:VIM-39, a VIM-1-like metallo-β-lactamase variant (VIM-1 Thr33Ala His224Leu) was identified in a clinical isolate of Klebsiella pneumoniae belonging to sequence type 147. VIM-39 hydrolyzed ampicillin, cephalothin, and imipenem more efficiently than did VIM-1 and VIM-26 (a VIM-1 variant with the His224Leu substitution) because of higher turnover rates.
ISSN:0066-4804
1098-6596
1098-6596
DOI:10.1128/AAC.01935-15