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. 2002 Feb;46(2):566-9.
doi: 10.1128/AAC.46.2.566-569.2002.

Integron-located oxa-32 gene cassette encoding an extended-spectrum variant of OXA-2 beta-lactamase from Pseudomonas aeruginosa

Laurent Poirel  1 , Patrick Gerome, Christophe De Champs, Jean Stephanazzi, Thierry Naas, Patrice Nordmann
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Integron-located oxa-32 gene cassette encoding an extended-spectrum variant of OXA-2 beta-lactamase from Pseudomonas aeruginosa

Laurent Poirel et al. Antimicrob Agents Chemother. 2002 Feb.

Abstract

Pseudomonas aeruginosa clinical isolate CY-1, which was resistant to ceftazidime, harbored a conjugative ca. 250-kb plasmid that contained a class 1 integron with two gene cassettes encoding OXA-32, an OXA-2- type beta-lactamase, and the aminoglycoside acetyltransferase AAC(6')Ib(9). OXA-32 differed from OXA-2 by an Leu169Ile amino acid substitution (class D numbering). Site-directed mutagenesis established that Ile169 is responsible for resistance to ceftazidime but not to cefotaxime.

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Figures

FIG. 1.
FIG. 1.
Comparison of the amino acid sequence of OXA-32 to those of OXA-15 and OXA-2. Dashes indicate identical amino acids. The numbering is according to the class D β-lactamase (DBL) numbering (2). The numbers of the amino acid positions involved in the extended-spectrum profile of either OXA-32 or OXA-15 are in boldface. The highlighted boxes indicate conserved regions within class D β-lactamases, and highly conserved residues are shown by asterisks.
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