CFE-1, a Novel Plasmid-Encoded AmpC β-Lactamase with an<i>ampR</i>Gene Originating from<i>Citrobacter freundii</i>

DOI Web Site 11 Citations
  • Ryuichi Nakano
    Department of Microbiology, School of Medicine and Environmental Infectious Disease, Graduate School of Medical Sciences, Kitasato University, Sagamihara, Kanagawa
  • Ryoichi Okamoto
    Department of Microbiology, School of Medicine and Environmental Infectious Disease, Graduate School of Medical Sciences, Kitasato University, Sagamihara, Kanagawa
  • Yumiko Nakano
    Department of Microbiology, School of Medicine and Environmental Infectious Disease, Graduate School of Medical Sciences, Kitasato University, Sagamihara, Kanagawa
  • Kenichi Kaneko
    Department of Microbiology, School of Medicine and Environmental Infectious Disease, Graduate School of Medical Sciences, Kitasato University, Sagamihara, Kanagawa
  • Naohiro Okitsu
    Department of Microbiology, School of Medicine and Environmental Infectious Disease, Graduate School of Medical Sciences, Kitasato University, Sagamihara, Kanagawa
  • Yoshio Hosaka
    Department of Microbiology, School of Medicine and Environmental Infectious Disease, Graduate School of Medical Sciences, Kitasato University, Sagamihara, Kanagawa
  • Matsuhisa Inoue
    Department of Microbiology, School of Medicine and Environmental Infectious Disease, Graduate School of Medical Sciences, Kitasato University, Sagamihara, Kanagawa

Abstract

<jats:title>ABSTRACT</jats:title><jats:p>A clinical isolate of<jats:italic>Escherichia coli</jats:italic>from a patient in Japan, isolate KU6400, was found to produce a plasmid-encoded β-lactamase that conferred resistance to extended-spectrum cephalosporins and cephamycins. Resistance arising from production of a β-lactamase could be transferred by either conjugation or transformation with plasmid pKU601 into<jats:italic>E. coli</jats:italic>ML4947. The substrate and inhibition profiles of this enzyme resembled those of the AmpC β-lactamase. The resistance gene of pKU601, which was cloned and expressed in<jats:italic>E. coli</jats:italic>, proved to contain an open reading frame showing 99.8% DNA sequence identity with the<jats:italic>ampC</jats:italic>gene of<jats:italic>Citrobacter freundii</jats:italic>GC3. DNA sequence analysis also identified a gene upstream of<jats:italic>ampC</jats:italic>whose sequence was 99.0% identical to the<jats:italic>ampR</jats:italic>gene from<jats:italic>C. freundii</jats:italic>GC3. In addition, a fumarate operon (<jats:italic>frdABCD</jats:italic>) and an outer membrane lipoprotein (<jats:italic>blc</jats:italic>) surrounding the<jats:italic>ampR-ampC</jats:italic>genes in<jats:italic>C. freundii</jats:italic>were identified, and insertion sequence (IS<jats:italic>26</jats:italic>) elements were observed on both sides of the sequences identified (forming an IS<jats:italic>26</jats:italic>composite transposon); these results confirm the evidence of the translocation of a β-lactamase-associated gene region from the chromosome to a plasmid. Finally, we describe a novel plasmid-encoded AmpC β-lactamase, CFE-1, with an<jats:italic>ampR</jats:italic>gene derived from<jats:italic>C. freundii</jats:italic>.</jats:p>

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