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JAC Advance Access originally published online on January 30, 2006
Journal of Antimicrobial Chemotherapy 2006 57(3):373-383; doi:10.1093/jac/dki482
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© The Author 2006. Published by Oxford University Press on behalf of the British Society for Antimicrobial Chemotherapy. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Review

OXA-type carbapenemases

Jan Walther-Rasmussen* and Niels Høiby

Department of Clinical Microbiology, 9301, Rigshospitalet, The National University Hospital, Copenhagen, Denmark

* Corresponding author. Tel: +45-35-45-64-29; Fax: +45-35-45-64-12; E-mail: jawalras{at}mail.tele.dk

In recent years, the number of class D ß-lactamases with carbapenem-hydrolysing properties has increased substantially. Based on amino acid sequence identities, these class D or OXA-type carbapenemases are divided into eight distantly related groups, and they are only remotely related to other class D ß-lactamases. A putative ancestor to one of the plasmid-encoded OXA-type carbapenemases has been found.

OXA-type carbapenemases are not integrated into integrons as gene cassettes like many class D oxacillinases, but most of the OXA-type carbapenemases are instead encoded by chromosomal genes. Some of these OXA-type carbapenemases are widely dispersed in Pseudomonas aeruginosa and especially in Acinetobacter baumannii.

Although most of the OXA-type carbapenemases show only weak carbapenemase activity, carbapenem resistance may result from a combined action an OXA-type carbapenemase and a secondary resistance mechanism such as porin deficiencies or overexpressed efflux pumps. This article reviews the phylogeny and the genetic environments of the encoding genes and kinetic properties of the OXA-type carbapenemases.

Keywords: class D ß-lactamases , carbapenem resistance , Acinetobacter baumannii , Pseudomonas aeruginosa


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