IMP-51, a novel IMP-type metallo-β-lactamase with increased doripenem- and meropenem-hydrolyzing activities, in a carbapenem-resistant Pseudomonas aeruginosa clinical isolate

Antimicrob Agents Chemother. 2015 Nov;59(11):7090-3. doi: 10.1128/AAC.01611-15. Epub 2015 Aug 17.

Abstract

A meropenem-resistant Pseudomonas aeruginosa isolate was obtained from a patient in a medical setting in Hanoi, Vietnam. The isolate was found to have a novel IMP-type metallo-β-lactamase, IMP-51, which differed from IMP-7 by an amino acid substitution (Ser262Gly). Escherichia coli expressing blaIMP-51 showed greater resistance to cefoxitin, meropenem, and moxalactam than E. coli expressing blaIMP-7. The amino acid residue at position 262 was located near the active site, proximal to the H263 Zn(II) ligand.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbapenems / pharmacology*
  • Cefoxitin / pharmacology
  • Doripenem
  • Escherichia coli / drug effects
  • Escherichia coli / enzymology
  • Meropenem
  • Microbial Sensitivity Tests
  • Moxalactam / pharmacology
  • Pseudomonas aeruginosa / drug effects*
  • Pseudomonas aeruginosa / enzymology
  • Thienamycins / pharmacology*
  • beta-Lactamases / genetics
  • beta-Lactamases / metabolism*

Substances

  • Carbapenems
  • Thienamycins
  • Cefoxitin
  • Doripenem
  • beta-Lactamases
  • Meropenem
  • Moxalactam