Characterisation of a unique ceftazidime-hydrolysing -lactamase, TEM-E2
| Autor: | Sebastian G. B. Amyes, M. S. Marriott, D. J. Payne |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Microbiology (medical)
Cefotaxime medicine.drug_class Cephalosporin Ceftazidime Penicillins Biology Microbiology beta-Lactamases Clavulanic Acids Klebsiella Clavulanic acid Escherichia coli medicine Cephaloridine Humans Clavulanic Acid Strain (chemistry) Hydrolysis Infant Newborn Drug Resistance Microbial Klebsiella oxytoca General Medicine Carbenicillin biology.organism_classification Cephalosporins Biochemistry Conjugation Genetic beta-Lactamase Inhibitors Plasmids medicine.drug |
| Zdroj: | Journal of Medical Microbiology. 32:131-134 |
| ISSN: | 1473-5644 0022-2615 |
| DOI: | 10.1099/00222615-32-2-131 |
| Popis: | A strain of Klebsiella oxytoca, originally isolated in Liverpool in 1982, has been found to produce a novel transferable beta-lactamase, TEM-E2. This enzyme confers resistance to ceftazidime and focused as a doublet band with an iso-electric point (pI) of 5.3. The strain also produced the TEM-1 beta-lactamase. Both TEM-1 and TEM-E2 beta-lactamases were encoded by a transferable 103 kb plasmid; these two enzymes also had similar molecular weights, were inhibited by clavulanic acid, and hydrolysed ampicillin, carbenicillin and cephaloridine at similar rates. However, unlike the TEM-1 enzyme, the TEM-E2 beta-lactamase hydrolysed ceftazidime and cefotaxime with similar efficiency, although it conferred much greater resistance to ceftazidime in the host strain. This is the earliest documented example of a TEM-like enzyme which confers transferable resistance to ceftazidime and related cephalosporins. |
| Databáze: | OpenAIRE |
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