NDM-4 metallo-β-lactamase with increased carbapenemase activity from Escherichia coli

Antimicrob Agents Chemother. 2012 Apr;56(4):2184-6. doi: 10.1128/AAC.05961-11. Epub 2012 Jan 17.

Abstract

A clinical Escherichia coli isolate resistant to all β-lactams, including carbapenems, expressed a novel metallo-β-lactamase (MBL), NDM-4, differing from NDM-1 by a single amino acid substitution (Met154Leu). NDM-4 possessed increased hydrolytic activity toward carbapenems and several cephalosporins compared to that of NDM-1. This amino acid substitution was not located in the known active sites of NDM-1, indicating that remote amino acid substitutions might also play a role in the extended activity of this MBL.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution
  • Anti-Bacterial Agents / pharmacology
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Carbapenems / pharmacology
  • Cephalosporins / pharmacology
  • Cloning, Molecular
  • DNA, Bacterial / genetics
  • Escherichia coli / drug effects
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Humans
  • Hydrolysis
  • Kinetics
  • Microbial Sensitivity Tests
  • Plasmids / genetics
  • Polymerase Chain Reaction
  • Urinary Tract Infections / microbiology
  • beta-Lactamases / genetics
  • beta-Lactamases / metabolism*

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Carbapenems
  • Cephalosporins
  • DNA, Bacterial
  • beta lactamase NDM-4, E coli
  • beta-Lactamases
  • carbapenemase