High-level resistance to ceftazidime conferred by a novel enzyme, CTX-M-32, derived from CTX-M-1 through a single Asp240-Gly substitution

Antimicrob Agents Chemother. 2004 Jun;48(6):2308-13. doi: 10.1128/AAC.48.6.2308-2313.2004.

Abstract

A clinical strain of Escherichia coli isolated from pleural liquid with high levels of resistance to cefotaxime, ceftazidime, and aztreonam harbors a novel CTX-M gene (bla(CTX-M-32)) whose amino acid sequence differs from that of CTX-M-1 by a single Asp240-Gly substitution. Moreover, by site-directed mutagenesis we demonstrated that this replacement is a key event in ceftazidime hydrolysis

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Ceftazidime / pharmacology*
  • Cephalosporin Resistance / genetics*
  • Cephalosporins / pharmacology*
  • DNA, Bacterial / genetics
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / drug effects*
  • Escherichia coli / genetics*
  • Escherichia coli Infections / microbiology
  • Isoelectric Focusing
  • Kinetics
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed / genetics
  • Plasmids / genetics
  • Pleura / microbiology
  • beta-Lactamases / genetics*

Substances

  • Cephalosporins
  • DNA, Bacterial
  • Ceftazidime
  • beta-lactamase TEM-3
  • beta-Lactamases
  • beta-lactamase CTX-M-32, E coli

Associated data

  • GENBANK/AJ557142