Unusual tazobactam-sensitive AmpC beta-lactamase from two Escherichia coli isolates
| Autor: | David M. Livermore, Susan D. Munro, Franck Danel, Gioia S. Babini, Patricia A. Micklesen |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Microbiology (medical)
Tazobactam medicine.medical_treatment Penicillanic Acid Ceftazidime Microbial Sensitivity Tests Biology medicine.disease_cause Benzylpenicillin beta-Lactamases Microbiology Bacterial Proteins Clavulanic acid Escherichia coli polycyclic compounds medicine Cephaloridine Pharmacology (medical) Enzyme Inhibitors Antibacterial agent Pharmacology biochemical phenomena metabolism and nutrition bacterial infections and mycoses Infectious Diseases Beta-lactamase bacteria medicine.drug |
| Zdroj: | Journal of Antimicrobial Chemotherapy. 41:115-118 |
| ISSN: | 1460-2091 0305-7453 |
| DOI: | 10.1093/jac/41.1.115 |
| Popis: | Two Escherichia coli isolates were studied. MIC patterns and hydrolysis assays suggested that they hyperproduced AmpC beta-lactamase, but synergy between ceftazidime and tazobactam was greater than between ceftazidime and Ro 48-1256, whereas the converse pattern is typical of AmpC hyperproducers. Studies with purified beta-lactamase from one of the isolates confirmed that tazobactam was a 100-fold stronger inhibitor than for the classical E. coli AmpC enzyme. Moreover, in contrast to typical AmpC types, the new enzyme had greater affinity for cephaloridine than for benzylpenicillin. |
| Databáze: | OpenAIRE |
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