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Mechanisms of Resistance

NDM-4 Metallo-β-Lactamase with Increased Carbapenemase Activity from Escherichia coli

Patrice Nordmann, Anne E. Boulanger, Laurent Poirel
Patrice Nordmann
Service de Bactériologie-Virologie, INSERM U914, Emerging Resistance to Antibiotics, Hôpital de Bicêtre, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine et Université Paris-Sud, Kremlin-Bicêtre, France
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Anne E. Boulanger
Service de Bactériologie-Virologie, INSERM U914, Emerging Resistance to Antibiotics, Hôpital de Bicêtre, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine et Université Paris-Sud, Kremlin-Bicêtre, France
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Laurent Poirel
Service de Bactériologie-Virologie, INSERM U914, Emerging Resistance to Antibiotics, Hôpital de Bicêtre, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine et Université Paris-Sud, Kremlin-Bicêtre, France
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DOI: 10.1128/AAC.05961-11
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ABSTRACT

A clinical Escherichia coli isolate resistant to all β-lactams, including carbapenems, expressed a novel metallo-β-lactamase (MBL), NDM-4, differing from NDM-1 by a single amino acid substitution (Met154Leu). NDM-4 possessed increased hydrolytic activity toward carbapenems and several cephalosporins compared to that of NDM-1. This amino acid substitution was not located in the known active sites of NDM-1, indicating that remote amino acid substitutions might also play a role in the extended activity of this MBL.

  • Copyright © 2012, American Society for Microbiology. All Rights Reserved.
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NDM-4 Metallo-β-Lactamase with Increased Carbapenemase Activity from Escherichia coli
Patrice Nordmann, Anne E. Boulanger, Laurent Poirel
Antimicrobial Agents and Chemotherapy Mar 2012, 56 (4) 2184-2186; DOI: 10.1128/AAC.05961-11

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NDM-4 Metallo-β-Lactamase with Increased Carbapenemase Activity from Escherichia coli
Patrice Nordmann, Anne E. Boulanger, Laurent Poirel
Antimicrobial Agents and Chemotherapy Mar 2012, 56 (4) 2184-2186; DOI: 10.1128/AAC.05961-11
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