Investigation of Oxacillin-Hydrolyzing Beta-Lactamase in Borderline Methicillin-Resistant Clinical Isolates of Staphylococcus aureus
| Autor: | Peter Kovacs, István Szabó, László Kiss, Attila Iglói, Ferenc Hernadi, Zsuzsanna Gál, György Barabás |
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| Rok vydání: | 2001 |
| Předmět: |
Pharmacology
Micrococcaceae Meticillin biology medicine.drug_class medicine.medical_treatment Antibiotics General Medicine biology.organism_classification medicine.disease_cause Microbiology Infectious Diseases Oncology Staphylococcus aureus Drug Discovery β lactams medicine Beta-lactamase Pharmacology (medical) Bacteria Antibacterial agent medicine.drug |
| Zdroj: | Chemotherapy. 47:233-238 |
| ISSN: | 1421-9794 0009-3157 |
| DOI: | 10.1159/000048528 |
| Popis: | Background: Mechanisms of borderline resistance of Staphylococcus aureus to penicillinase-resistant penicillins (PRPs) may include hyperproduction of classical penicillinase and/or production of β-lactamase hydrolyzing also PRPs. Methods: β-Lactamase activity of whole cells and purified enzymes was estimated spectrophotometrically and in isolated cytoplasmic membranes by bioassay with Bacillus subtilis as test strain. Results: Out of 53 clinical isolates of S. aureus, 18 showed oxacillin MIC values from 0.5 to 2 µg/ml, which were reduced by sulbactam and/or clavulanic acid in the case of four isolates producing large quantities of inducible, type A β-lactamase. Cytoplasmic membranes isolated from these strains showed oxacillin-hydrolyzing activity. One of these strains was grown also in the presence of globomycin, an antibiotic known to interfere with the anchorage of membrane lipoproteins; this treatment eliminated the oxacillin-hydrolyzing activity. Conclusions: The resistance in these strains was due to a membrane-bound lipoprotein with oxacillin-hydrolyzing activity. |
| Databáze: | OpenAIRE |
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