CMY-42, a novel plasmid-mediated CMY-2 variant AmpC beta-lactamase

Microb Drug Resist. 2011 Jun;17(2):165-9. doi: 10.1089/mdr.2010.0137. Epub 2011 Mar 9.

Abstract

We isolated a clinical Escherichia coli strain with an antimicrobial resistance phenotype characteristic for the expression of an AmpC beta-lactamase. Molecular methods revealed a novel, plasmid-localized variant of CMY-2 with a substitution of valine 231 for serine (V231S), which was designated CMY-42. Like the CMY-2-like AmpC beta-lactamase CMY-30, carrying the substitution V231G, CMY-42 displayed increased activity toward expanded spectrum cephalosporins. This finding supports the hypothesis that a bulky side chain at position 231 (Ambler's position 211) may pose a steric clash with certain cephalosporins hindering the access of the AmpC beta-lactamase; however, additional phenomena may account for the observed hydrolytic properties.

MeSH terms

  • Anti-Bacterial Agents / pharmacology*
  • Cephalosporins / pharmacology*
  • Drug Resistance, Bacterial / drug effects
  • Drug Resistance, Bacterial / genetics*
  • Escherichia coli Infections / drug therapy
  • Escherichia coli Infections / genetics
  • Escherichia coli Infections / microbiology*
  • Escherichia coli Proteins / genetics*
  • Escherichia coli Proteins / metabolism
  • Escherichia coli* / genetics
  • Escherichia coli* / growth & development
  • Escherichia coli* / isolation & purification
  • Humans
  • Molecular Sequence Data
  • Plasmids / genetics*
  • Plasmids / metabolism
  • Serine / genetics
  • Serine / metabolism
  • Surgical Wound Infection / drug therapy
  • Surgical Wound Infection / genetics
  • Surgical Wound Infection / microbiology*
  • Valine / genetics
  • Valine / metabolism
  • beta-Lactamases / genetics*
  • beta-Lactamases / metabolism

Substances

  • Anti-Bacterial Agents
  • Cephalosporins
  • Escherichia coli Proteins
  • Serine
  • beta-lactamase CMY-2
  • beta-Lactamases
  • beta-lactamase CMY-42, E coli
  • Valine