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Characterisation of a unique ceftazidime-hydrolysing beta-lactamase, TEM-E2
D J Payne1, M S Marriott, S G Amyes
1Department of Bacteriology, Medical School, University of Edinburgh.
Journal of Medical Microbiology
|June 1, 1990
Summary
Researchers discovered a new transferable beta-lactamase, TEM-E2, in Klebsiella oxytoca. This enzyme provides resistance to ceftazidime, marking an early instance of transferable cephalosporin resistance.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Klebsiella oxytoca is an opportunistic pathogen.
- Beta-lactamase enzymes confer resistance to beta-lactam antibiotics.
- The emergence of antibiotic resistance is a significant global health concern.
Purpose of the Study:
- To characterize a novel beta-lactamase produced by Klebsiella oxytoca.
- To investigate the genetic basis of transferable antibiotic resistance.
- To determine the enzymatic properties and substrate profile of the novel enzyme.
Main Methods:
- Bacterial isolation and identification.
- Plasmid DNA extraction and characterization.
- Enzyme purification and kinetic analysis.
- Antibiotic susceptibility testing.
Main Results:
- A novel transferable beta-lactamase, TEM-E2, was identified in Klebsiella oxytoca.
- TEM-E2 confers resistance to ceftazidime and cefotaxime.
- Both TEM-1 and TEM-E2 beta-lactamases were encoded on a transferable 103 kb plasmid.
- TEM-E2 demonstrated efficient hydrolysis of ceftazidime and cefotaxime, conferring significant resistance.
Conclusions:
- This study reports the earliest documented TEM-like enzyme conferring transferable resistance to ceftazidime.
- The discovery of TEM-E2 highlights the evolving mechanisms of antibiotic resistance in Klebsiella species.
- Understanding novel beta-lactamases is crucial for developing effective antimicrobial strategies.