Genetic and Functional Variability of AmpC-Type β-Lactamases from <i>Acinetobacter baumannii</i>

  • José-Manuel Rodríguez-Martínez
    Service de Bactériologie-Virologie, INSERM U914 Emerging Resistance to Antibiotics, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine, and Université Paris-Sud, Hôpital de Bicêtre, 94275 K.-Bicêtre, France
  • Laurent Poirel
    Service de Bactériologie-Virologie, INSERM U914 Emerging Resistance to Antibiotics, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine, and Université Paris-Sud, Hôpital de Bicêtre, 94275 K.-Bicêtre, France
  • Patrice Nordmann
    Service de Bactériologie-Virologie, INSERM U914 Emerging Resistance to Antibiotics, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine, and Université Paris-Sud, Hôpital de Bicêtre, 94275 K.-Bicêtre, France

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<jats:title>ABSTRACT</jats:title> <jats:p> The incidence of naturally occurring AmpC β-lactamases with extended activities toward several cephalosporins was evaluated among 17 ceftazidime (CAZ)-resistant <jats:italic>Acinetobacter baumannii</jats:italic> isolates. Five AmpC β-lactamases (named ADC β-lactamases) were identified, among which those possessing the Val208Ala (inside the omega-loop) or Asn283Ser (helix H-10) substitution conferred higher levels of resistance (4- to 64-fold higher) to CAZ and to cefotaxime in <jats:italic>Escherichia coli</jats:italic> . This study demonstrates that peculiar AmpCs playing a role in resistance to broad-spectrum cephalosporins in <jats:italic>A. baumannii</jats:italic> may be identified. </jats:p>

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