Characterization of metallo-beta-lactamase VIM-27, an A57S mutant of VIM-1 associated with Klebsiella pneumoniae ST147

Antimicrob Agents Chemother. 2011 Jul;55(7):3570-2. doi: 10.1128/AAC.00238-11. Epub 2011 Apr 25.

Abstract

VIM-27 metallo-β-lactamase, an Ala(57) → Ser variant of VIM-1, was identified in three Klebsiella pneumoniae isolates belonging to sequence type 147. bla(VIM-27) was part of a class 1 integron carried by non-self-transferable plasmids. Kinetic parameters and MIC determinations indicated that VIM-27 hydrolyzed most β-lactams, especially imipenem and cefoxitin, less effectively than VIM-1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Cefoxitin / pharmacology
  • Drug Resistance, Multiple, Bacterial / genetics
  • Imipenem / pharmacology
  • Klebsiella pneumoniae / drug effects
  • Klebsiella pneumoniae / enzymology*
  • Klebsiella pneumoniae / genetics
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Molecular Structure
  • beta-Lactamases / chemistry*
  • beta-Lactamases / genetics
  • beta-Lactamases / metabolism*

Substances

  • Anti-Bacterial Agents
  • Cefoxitin
  • Imipenem
  • VIM-1 metallo-beta-lactamase
  • beta-Lactamases

Associated data

  • GENBANK/HQ858608