Increase in beta-lactam-resistant Proteus mirabilis strains due to CTX-M- and CMY-type as well as new VEB- and inhibitor-resistant TEM-type beta-lactamases

J Antimicrob Chemother. 2008 May;61(5):1029-32. doi: 10.1093/jac/dkn056. Epub 2008 Feb 20.

Abstract

Objectives: The aim of this study was to characterize the different inhibitor-resistant TEM beta-lactamases, extended-spectrum beta-lactamases (ESBLs) and plasmid-mediated AmpC beta-lactamases implicated in beta-lactam resistance in Proteus mirabilis, which has increased over recent years.

Methods: From February 2000 to December 2005, 1423 clinical isolates of P. mirabilis were collected. The AmpC phenotype was checked by means of a double-disc synergy test using cloxacillin as an inhibitor of AmpC enzymes. The production of ESBL was assessed by the double-disc synergy method and by Etest ESBL. Analytical isoelectric focusing, determination of kinetic constants, conjugation, PCR and a sequencing strategy were used to characterize the enzymes. The possible relationships between isolates were analysed by PFGE.

Results and conclusions: Twenty-five of 1423 isolates were found to display intermediate or full resistance to co-amoxiclav, cefotaxime or ceftazidime. Seventeen isolates had reduced susceptibility to co-amoxiclav; of these, seven produced TEM-110, eight produced the new TEM-159, one the new TEM-160 and one TEM-1. Five isolates producing TEM-110, TEM-159 or TEM-160 enzymes shared the same PFGE profile. Three isolates produced an ESBL, CTX-M-1, CTX-M-32 and the new variant, VEB-4. Finally, five isolates with an AmpC phenotype produced CMY-2, two with the same PFGE profile. Our data emphasize the diversity of beta-lactamases found in this species.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution
  • Anti-Bacterial Agents / pharmacology*
  • Gene Expression Regulation, Bacterial
  • Humans
  • Proteus Infections / microbiology
  • Proteus mirabilis / drug effects*
  • Proteus mirabilis / metabolism
  • beta-Lactam Resistance / genetics*
  • beta-Lactamase Inhibitors
  • beta-Lactamases / chemistry
  • beta-Lactamases / genetics
  • beta-Lactamases / metabolism*

Substances

  • Anti-Bacterial Agents
  • beta-Lactamase Inhibitors
  • beta-Lactamases