Characterisation of a unique ceftazidime-hydrolysing beta-lactamase, TEM-E2

J Med Microbiol. 1990 Jun;32(2):131-4. doi: 10.1099/00222615-32-2-131.

Abstract

A strain of Klebsiella oxytoca, originally isolated in Liverpool in 1982, has been found to produce a novel transferable beta-lactamase, TEM-E2. This enzyme confers resistance to ceftazidime and focused as a doublet band with an iso-electric point (pI) of 5.3. The strain also produced the TEM-1 beta-lactamase. Both TEM-1 and TEM-E2 beta-lactamases were encoded by a transferable 103 kb plasmid; these two enzymes also had similar molecular weights, were inhibited by clavulanic acid, and hydrolysed ampicillin, carbenicillin and cephaloridine at similar rates. However, unlike the TEM-1 enzyme, the TEM-E2 beta-lactamase hydrolysed ceftazidime and cefotaxime with similar efficiency, although it conferred much greater resistance to ceftazidime in the host strain. This is the earliest documented example of a TEM-like enzyme which confers transferable resistance to ceftazidime and related cephalosporins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cefotaxime / metabolism
  • Ceftazidime / metabolism*
  • Ceftazidime / pharmacology
  • Cephalosporins / metabolism
  • Cephalosporins / pharmacology
  • Clavulanic Acid
  • Clavulanic Acids / pharmacology
  • Conjugation, Genetic
  • Drug Resistance, Microbial
  • Escherichia coli / drug effects
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Humans
  • Hydrolysis
  • Infant, Newborn
  • Klebsiella / drug effects
  • Klebsiella / enzymology*
  • Klebsiella / genetics
  • Penicillins / metabolism
  • Penicillins / pharmacology
  • Plasmids
  • beta-Lactamase Inhibitors
  • beta-Lactamases / genetics
  • beta-Lactamases / metabolism*

Substances

  • Cephalosporins
  • Clavulanic Acids
  • Penicillins
  • beta-Lactamase Inhibitors
  • Clavulanic Acid
  • Ceftazidime
  • beta-Lactamases
  • beta-lactamase TEM-2
  • Cefotaxime