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Antimicrob Agents Chemother. 2012 Apr;56(4):2184-6. doi: 10.1128/AAC.05961-11. Epub 2012 Jan 17.

NDM-4 metallo-β-lactamase with increased carbapenemase activity from Escherichia coli.

Author information

1
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. nordmann.patrice@bct.aphp.fr

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.

PMID:
22252797
PMCID:
PMC3318389
DOI:
10.1128/AAC.05961-11
[Indexed for MEDLINE]
Free PMC Article

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