Carbapenem inactivation method using bacterial lysate and MOPS (LCIM): a very sensitive method for detecting carbapenemase-producing Acinetobacter species

J Antimicrob Chemother. 2020 Oct 1;75(10):2812-2816. doi: 10.1093/jac/dkaa238.

Abstract

Objectives: Detection of carbapenem-hydrolysing class D β-lactamase (CHDL)-producing Acinetobacter spp. is critical for understanding antibiotic resistance. In this study, we compared the available detection techniques derived from the carbapenem inactivation method (CIM), using CHDL-producing Acinetobacter spp., and developed a modified method that uses bacterial lysate (lysate CIM; LCIM).

Methods: A total of 159 Acinetobacter spp. (102 carbapenemase producers and 57 non-producers) and 14 Pseudomonas spp. (7 carbapenemase producers and 7 non-producers) were tested. Modified CIM, simplified CIM, CIMTris, Triton-CIM and LCIM were compared using these strains. Distinct from the CIM, LCIM includes a longer incubation period (4 h) with 2.0% Triton X-100 (v/v) in 20 mM MOPS buffer instead of water.

Results: The sensitivity/specificity of the modified CIM, simplified CIM, CIMTris, Triton-CIM and LCIM were 71.6%/100%, 66.1%/89.1%, 88.1%/95.3%, 80.7%/100% and 97.2%/100%, respectively. LCIM was the most sensitive and specific.

Conclusions: Use of bacterial lysate and MOPS increased the sensitivity of the CIM in detecting CHDL-producing Acinetobacter spp.

MeSH terms

  • Acinetobacter* / drug effects
  • Acinetobacter* / genetics
  • Anti-Bacterial Agents* / pharmacology
  • Bacterial Proteins* / metabolism
  • Carbapenems* / pharmacology
  • Cell Extracts
  • Microbial Sensitivity Tests
  • Morpholines
  • Sensitivity and Specificity
  • beta-Lactamases* / metabolism

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Broncho-Vaxom
  • Carbapenems
  • Cell Extracts
  • Morpholines
  • morpholinopropane sulfonic acid
  • beta-Lactamases
  • carbapenemase