Biochemical and genetic characterization of carbapenem-hydrolyzing β-lactamase OXA-229 from Acinetobacter bereziniae

Antimicrob Agents Chemother. 2012 Jul;56(7):3923-7. doi: 10.1128/AAC.00257-12. Epub 2012 Apr 16.

Abstract

Acinetobacter bereziniae (formerly Acinetobacter genomospecies 10) isolate Nec was recovered from a skin sample of a patient hospitalized in Paris, France. It was resistant to penicillins, penicillin-inhibitor combinations, and carbapenems. Cloning and expression in Escherichia coli identified the carbapenem-hydrolyzing class D β-lactamase OXA-229, which is weakly related to other oxacillinases (66% amino acid identity with the closest oxacillinase, OXA-58). It hydrolyzed penicillins, oxacillin, and imipenem but not expanded-spectrum cephalosporins. Sequencing of the genetic context of the bla(OXA-229) gene did not identify an insertion sequence but did identify mutations in the promoter sequences in comparison to the fully susceptible A. bereziniae reference strain. The overexpression of bla(OXA-229) in A. bereziniae Nec as a source of carbapenem resistance was identified by quantitative real-time PCR.

MeSH terms

  • Acinetobacter / drug effects
  • Acinetobacter / enzymology*
  • Acinetobacter / genetics
  • Carbapenems / metabolism*
  • Kanamycin / pharmacology
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Mutation
  • Phylogeny
  • Real-Time Polymerase Chain Reaction
  • Ticarcillin / pharmacology
  • Transcription Initiation Site
  • beta-Lactamases / classification
  • beta-Lactamases / genetics
  • beta-Lactamases / metabolism*

Substances

  • Carbapenems
  • Kanamycin
  • beta-Lactamases
  • Ticarcillin

Associated data

  • GENBANK/JQ422052
  • GENBANK/JQ422053
  • GENBANK/JQ422054