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Future Microbiol. 2007 Oct;2(5):501-12.

Carbapenemases: molecular diversity and clinical consequences.

Author information

1
Université Paris XI, Service de Bactériologie-Virologie, Hôpital de Bicêtre, Assistance Punblique/Hôpitaux de Paris, Faculté de Médecine Paris-Sud, 94275 K.-Bicêtre, France. laurent.poirel@bct.aphp.fr

Abstract

Carbapenemases are beta-lactamases that hydrolyze most beta-lactams including carbapenems. Carbapenemases are classified in four molecular classes; those belonging to class A are the chromosomally-encoded and clavulanic acid-inhibited IMI, NMC-A and SME, identified in Enterobacter cloacae and Serratia marcescens; the plasmid-encoded KPC enzymes identified in Enterobacteriaceae (and rarely in Pseudomonas aeruginosa); and the GES-type enzymes identified in Enterobacteriaceae and P. aeruginosa. The class B enzymes are the most clinically-significant carbapenemases; they are metallo-beta-lactamases, mostly of the IMP and the VIM series. They have been reported worldwide and their genes are plasmid- and integron-located, hydrolyzing all beta-lactams with the exception of aztreonam. One single plasmid-mediated AmpC beta-lactamase, CMY-10, identified in an Enterobacter aerogenes isolate, has been shown to be a cephaslosporinase with some carbapenemase properties. Finally, the class D carbapenemases are being increasingly reported, mostly in Acinetobacter baumannii, and they compromise the efficacy of imipenem and meropenem significantly.

PMID:
17927473
DOI:
10.2217/17460913.2.5.501
[Indexed for MEDLINE]

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