A model system to demonstrate that beta-lactamase-associated antibiotic trapping could be a potential means of resistance

J Infect Dis. 1983 Aug;148(2):316-21. doi: 10.1093/infdis/148.2.316.

Abstract

Addition of beta-lactamase to 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 beta-lactam antibiotic (oxacillin), which had a higher affinity for the beta-lactamase 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 play a role in the resistance of some gram-negative bacteria to third-generation cephalosporins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cefotaxime / analogs & derivatives
  • Cefotaxime / metabolism
  • Cefotaxime / pharmacology
  • Ceftriaxone
  • Cephalosporins / pharmacology*
  • Cephalothin / metabolism
  • Cephalothin / pharmacology
  • Enterobacter / drug effects*
  • Enterobacter / enzymology
  • Enterobacteriaceae / drug effects*
  • Escherichia coli / drug effects*
  • Oxacillin / metabolism
  • Oxacillin / pharmacology*
  • Penicillin Resistance
  • beta-Lactamase Inhibitors
  • beta-Lactamases / metabolism*

Substances

  • Cephalosporins
  • beta-Lactamase Inhibitors
  • Ceftriaxone
  • beta-Lactamases
  • Cefotaxime
  • Cephalothin
  • Oxacillin