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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetyltransferases / metabolism
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Amino Acid Sequence
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Cefotaxime / pharmacology
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Ceftazidime / pharmacology
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Cephalosporins / pharmacology
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Drug Resistance, Bacterial / physiology
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Humans
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Pseudomonas aeruginosa / drug effects
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Pseudomonas aeruginosa / enzymology*
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Pseudomonas aeruginosa / genetics
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Sequence Homology, Amino Acid
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beta-Lactamases / genetics*
Substances
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Cephalosporins
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Ceftazidime
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Acetyltransferases
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aminoglycoside N(6')-acetyltransferase
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beta-lactamase OXA-2
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beta-Lactamases
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Cefotaxime