Loss of the 29-kilodalton outer membrane protein in the presence of OXA-51-like enzymes in Acinetobacter baumannii is associated with decreased imipenem susceptibility

Microb Drug Resist. 2009 Sep;15(3):151-8. doi: 10.1089/mdr.2009.0828.

Abstract

Carbapenem resistance in Acinetobacter baumannii is increasing these days. We investigated the roles of outer membrane proteins and efflux pumps in carbapenem resistance of A. baumannii which showed no carbapenemase activity in modified Hodge test. Among 58 carbapenem-resistant isolates collected from the Korea University Medical Center between January 2002 and March 2006, 17 isolates showed negative results in modified Hodge test. In outer membrane protein analysis, loss of the 29-kDa protein band was related with higher imipenem minimum inhibitory concentrations especially in the presence of OXA-51-like enzymes. Efflux pump-mediated carbapenem resistance was found in one out of the 17 isolates (5.9%). All of the 58 carbapenem-resistant strains and 5 of the 10 carbapenem-susceptible strains had OXA-51-like carbapenemase genes, suggesting that OXA-51-like enzymes may be naturally existing in A. baumannii and have very weak carbapenem hydrolyzing activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Academic Medical Centers
  • Acinetobacter Infections / microbiology
  • Acinetobacter baumannii / drug effects*
  • Acinetobacter baumannii / enzymology
  • Acinetobacter baumannii / genetics
  • Acinetobacter baumannii / isolation & purification
  • Anti-Bacterial Agents / pharmacology*
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Drug Resistance, Bacterial
  • Humans
  • Imipenem / pharmacology*
  • Korea
  • Microbial Sensitivity Tests
  • Random Amplified Polymorphic DNA Technique
  • beta-Lactamases / genetics*
  • beta-Lactamases / metabolism

Substances

  • 29-kDa outer membrane protein, Acinetobacter baumannii
  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Imipenem
  • beta-Lactamases
  • carbapenemase