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. 2011 Oct;55(10):4896-9.
doi: 10.1128/AAC.00481-11. Epub 2011 Jul 18.

Characterization of OXA-181, a carbapenem-hydrolyzing class D beta-lactamase from Klebsiella pneumoniae

Anaïs Potron  1 , Patrice Nordmann, Emilie Lafeuille, Zaina Al Maskari, Fatma Al Rashdi, Laurent Poirel
Affiliations

Characterization of OXA-181, a carbapenem-hydrolyzing class D beta-lactamase from Klebsiella pneumoniae

Anaïs Potron et al. Antimicrob Agents Chemother. 2011 Oct.

Abstract

Klebsiella pneumoniae KP3 was isolated from a patient transferred from India to the Sultanate of Oman. K. pneumoniae KP3 was resistant to all β-lactams, including carbapenems, and expressed the carbapenem-hydrolyzing β-lactamase OXA-181, which differs from OXA-48 by four amino acid substitutions. Compared to OXA-48, OXA-181 possessed a very similar hydrolytic profile. The bla(OXA-181) gene was located on a 7.6-kb ColE-type plasmid and was linked to the insertion sequence ISEcp1. The ISEcp1-mediated one-ended transposition of bla(OXA-181) was also demonstrated.

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Figures

Fig. 1.
Fig. 1.
Schematic map of the structure of transposon Tn2013. Open reading frames are shown as arrows or horizontal boxes with an arrow indicating the orientation of the coding sequence. The IRL, IRR1, and IRR2 motifs are indicated (black base pairs are identical, and white base pairs are different), and target site duplications (ATATA) are represented by black bars.
Fig. 2.
Fig. 2.
Map of natural plasmid pKP3-A harboring the blaOXA-181 gene. Coding regions are indicated by arrows showing the direction of transcription.
See this image and copyright information in PMC

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