Characterization of a new extended-spectrum beta-lactamase (TEM-87) isolated in Proteus mirabilis during an Italian survey

Antimicrob Agents Chemother. 2002 Mar;46(3):925-8. doi: 10.1128/AAC.46.3.925-928.2002.

Abstract

A new natural TEM derivative, named TEM-87, was identified in a Proteus mirabilis isolate from an Italian hospital. Compared to TEM-1, TEM-87 contains the following mutations: E104K, R164C, and M182T. Kinetic analysis of TEM-87 revealed extended-spectrum activity against oxyimino cephalosporins (preferentially ceftazidime) and aztreonam. Expression of blaTEM-87 in Escherichia coli decreased the host susceptibility to these drugs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aztreonam / pharmacology
  • Cephalosporins / metabolism
  • Escherichia coli / drug effects
  • Escherichia coli / genetics
  • Humans
  • Italy / epidemiology
  • Kinetics
  • Molecular Sequence Data
  • Monobactams / pharmacology
  • Proteus Infections / epidemiology*
  • Proteus Infections / microbiology*
  • Proteus mirabilis / enzymology*
  • Reverse Transcriptase Polymerase Chain Reaction
  • beta-Lactamases / analysis
  • beta-Lactamases / isolation & purification
  • beta-Lactamases / metabolism*

Substances

  • Cephalosporins
  • Monobactams
  • beta-lactamase TEM-87
  • beta-Lactamases
  • Aztreonam

Associated data

  • GENBANK/AF250872