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Mechanisms of Resistance

Genetic and Biochemical Characterization of the First Extended-Spectrum CARB-Type ß-Lactamase, RTG-4, from Acinetobacter baumannii

Anaïs Potron, Laurent Poirel, Jacques Croizé, Vanessa Chanteperdrix, Patrice Nordmann
Anaïs Potron
1Service de Bactériologie-Virologie, INSERM U914, Emerging Resistance to Antibiotics, Hôpital de Bicêtre, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine et Université Paris-Sud, Le Kremlin-Bicêtre
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Laurent Poirel
1Service de Bactériologie-Virologie, INSERM U914, Emerging Resistance to Antibiotics, Hôpital de Bicêtre, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine et Université Paris-Sud, Le Kremlin-Bicêtre
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Jacques Croizé
2Département de Microbiologie, CHU de Grenoble, Faculté de Médecine, Université Joseph Fourier, Grenoble, France
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Vanessa Chanteperdrix
2Département de Microbiologie, CHU de Grenoble, Faculté de Médecine, Université Joseph Fourier, Grenoble, France
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Patrice Nordmann
1Service de Bactériologie-Virologie, INSERM U914, Emerging Resistance to Antibiotics, Hôpital de Bicêtre, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine et Université Paris-Sud, Le Kremlin-Bicêtre
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  • For correspondence: nordmann.patrice@bct.aphp.fr
DOI: 10.1128/AAC.01164-08
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ABSTRACT

Acinetobacter baumannii isolate KAR was uncommonly more resistant to cefepime and cefpirome than to ceftazidime and cefotaxime. Cloning and expression of the β-lactamase gene content of this isolate into Escherichia coli TOP10 identified ß-lactamase RTG-4 (or CARB-10), which corresponds to the first reported extended-spectrum CARB-type enzyme. RTG-4 is a plasmid-encoded Ambler class A β-lactamase whose sequence differs by 4 amino acid substitutions from the narrow-spectrum β-lactamase RTG-3. RTG-4 hydrolyzes cefepime and cefpirome and weakly hydrolyzes ceftazidime due to the single Ser-to-Thr substitution at Ambler position 69. RTG-4 is less susceptible to inhibition by tazobactam and sulbactam than RTG-3. Expression of β-lactamase RTG-4 in a wild-type A. baumannii reference strain showed that it conferred resistance to cefepime and cefpirome. The genetic environment of the blaRTG-4 gene was made of a peculiar transposon located on a ca. 50-kb plasmid. ISAba9, located upstream of blaRTG-4, may be responsible for its acquisition by recognizing a secondary right inverted repeat sequence, thus acting by a one-ended transposition process.

  • Copyright © 2009 American Society for Microbiology
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Genetic and Biochemical Characterization of the First Extended-Spectrum CARB-Type ß-Lactamase, RTG-4, from Acinetobacter baumannii
Anaïs Potron, Laurent Poirel, Jacques Croizé, Vanessa Chanteperdrix, Patrice Nordmann
Antimicrobial Agents and Chemotherapy Jun 2009, 53 (7) 3010-3016; DOI: 10.1128/AAC.01164-08

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Genetic and Biochemical Characterization of the First Extended-Spectrum CARB-Type ß-Lactamase, RTG-4, from Acinetobacter baumannii
Anaïs Potron, Laurent Poirel, Jacques Croizé, Vanessa Chanteperdrix, Patrice Nordmann
Antimicrobial Agents and Chemotherapy Jun 2009, 53 (7) 3010-3016; DOI: 10.1128/AAC.01164-08
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KEYWORDS

Acinetobacter baumannii
beta-lactamases

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