Novel, plasmid-encoded, TEM-derived extended-spectrum beta-lactamase in Klebsiella pneumoniae conferring higher resistance to aztreonam than to extended-spectrum cephalosporins

Antimicrob Agents Chemother. 1993 Sep;37(9):2020-3. doi: 10.1128/AAC.37.9.2020.

Abstract

A clinical isolate of Klebsiella pneumoniae was more resistant to aztreonam than to cefotaxime and ceftazidime. It produced a clavulanate-susceptible beta-lactamase with an isoelectric point of 6.3 which readily hydrolyzed penicillins, cefotaxime, and ceftazidime, but which hydrolyzed aztreonam poorly. The enzyme was encoded by a gene on a 15-kb plasmid; the gene hybridized with an intragenic DNA probe of blaTEM.

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Aztreonam / pharmacology*
  • Cephalosporins / pharmacology*
  • DNA Probes
  • DNA, Bacterial / biosynthesis
  • Humans
  • Isoelectric Focusing
  • Kinetics
  • Klebsiella Infections / microbiology
  • Klebsiella pneumoniae / drug effects*
  • Klebsiella pneumoniae / enzymology
  • Klebsiella pneumoniae / genetics
  • Phenotype
  • Plasmids
  • beta-Lactamase Inhibitors
  • beta-Lactamases / genetics
  • beta-Lactamases / metabolism*

Substances

  • Anti-Bacterial Agents
  • Cephalosporins
  • DNA Probes
  • DNA, Bacterial
  • beta-Lactamase Inhibitors
  • beta-lactamase TEM-3
  • beta-Lactamases
  • Aztreonam