A Model System to Demonstrate That -Lactamase-Associated Antibiotic Trapping Could Be a Potential Means of Resistance
- 31 July 1983
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Infectious Diseases
- Vol. 148 (2), 316-321
- https://doi.org/10.1093/infdis/148.2.316
Abstract
Addition of β-Iactamaseto cultures of antibiotic-sensitive Escherichia coli protected the bacteria against lysis induced by either a hydrolyzable (cephalothin) or relatively nonhydrolyzable (ceftriaxone) cephalosporin. The later addition of a nonhydrolyzable, non-lysis-inducing β-Iactam antibiotic (oxacillin), which had a higher affinity for the β-Iactamase than ceftriaxone, allowed the reversal of the protection and the onset of lysis. These results suggest that trapping of the antibiotic by the enzyme, without significant hydrolysis, is a reversible process that may playa role in the resistance of some gram-negative bacteria to third-generation cephalosporins.Keywords
This publication has 3 references indexed in Scilit:
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- Moxalactam therapy of infections caused by cephalothin-resistant bacteria: influence of serum inhibitory activity on clinical response and acquisition of antibiotic resistance during therapyAntimicrobial Agents and Chemotherapy, 1981
- Insensitivity of peptidoglycan biosynthetic reactions to beta-lactam antibiotics in a clinical isolate of Pseudomonas aeruginosaAntimicrobial Agents and Chemotherapy, 1981