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Journal of Antimicrobial Chemotherapy (1987) 20, 7-13
© 1987 The British Society for Antimicrobial Chemotherapy

research-article

‘Covalent trapping’ and latamoxef resistance in ß-lactamase-derepressed Pseudomonas aeruginosa

D. M. Livermore

Department of Medical Microbiology, London Hospital Medical College Turner Street, London E1 2AD, UK

accepted 15 February 1987

Three Pseudomonas aeruginosa strains which constitutively produced chromosomal (Id, or Sabath and Abraham) ß-lactamase in large amounts were resistant to latamoxef (moxalactam) MICs, 128–256 mg/l). Their ß-lactamase-basal mutants, which produced 1200–18,000-fold less enzyme, were latamoxef-sensitive (MICs, 4–16 mg/l), suggesting that the enzyme caused the resistance of the parent organisms. Latamoxef was a feeble substrate of the enzyme (kcal <0.5/min) but reacted to form a stable complex that lacked catalytic activity against benzylpenicillin. The complex was isolated by gel filtration and was shown to be stable to isoelectric focusing, suggesting a covalent link between the enzyme and latamoxef. During incubation the complex underwent a slow breakdown, regenerating active enzyme. This breakdown obeyed first-order kinetics, and the half-life of the inactivated form was 19±1min at 37°C. Binding of antibiotic molecules in this complex may contribute to the latamoxef-resistance observed in the ß-lactamase-derepressed strains. This ‘covalent trapping’ should be distinguished from the ‘non-covalent trapping’ proposed elsewhere as a general mechanism of ß-lactamase-mediated resistance to reversibly-bound weak-substrate ß-lactams.


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