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Journal Article | Research Support, Non-U.S. Gov't

OXA-18, a class D clavulanic acid-inhibited extended-spectrum beta-lactamase from Pseudomonas aeruginosa.

L N Philippon, T Naas, A T Bouthors, V Barakett, P Nordmann
L N Philippon
Service de Bactériologie-Virologie, Hôpital Antoine Béclère, Faculté de Médecine Paris-Sud, Clamart, France.
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T Naas
Service de Bactériologie-Virologie, Hôpital Antoine Béclère, Faculté de Médecine Paris-Sud, Clamart, France.
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A T Bouthors
Service de Bactériologie-Virologie, Hôpital Antoine Béclère, Faculté de Médecine Paris-Sud, Clamart, France.
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V Barakett
Service de Bactériologie-Virologie, Hôpital Antoine Béclère, Faculté de Médecine Paris-Sud, Clamart, France.
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P Nordmann
Service de Bactériologie-Virologie, Hôpital Antoine Béclère, Faculté de Médecine Paris-Sud, Clamart, France.
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DOI: 10.1128/AAC.41.10.2188
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ABSTRACT

Clinical isolate Pseudomonas aeruginosa Mus showed resistance both to extended-spectrum cephalosporins and to aztreonam. We detected a typical double-disk synergy image when ceftazidime or aztreonam was placed next to a clavulanic acid disk on an agar plate. This resistance phenotype suggested the presence of an extended-spectrum beta-lactamase. Isoelectric focusing revealed that this strain produced three beta-lactamases, of pI 5.5, 7.4, and 8.2. A 2.6-kb Sau3A fragment encoding the extended-spectrum beta-lactamase of pI 5.5 was cloned from P. aeruginosa Mus genomic DNA. This enzyme, named OXA-18, had a relative molecular mass of 30.6 kDa. OXA-18 has a broad substrate profile, hydrolyzing amoxicillin, ticarcillin, cephalothin, ceftazidime, cefotaxime, and aztreonam, but not imipenem or cephamycins. Its activity was totally inhibited by clavulanic acid at 2 microg/ml. Hydrolysis constants of OXA-18 (Vmax, Km) confirmed the MIC results. Cloxacillin and oxacillin hydrolysis was noticeable with the partially purified OXA-18. The blaOXA-18 gene encodes a 275-amino-acid protein which has weak identity with all class D beta-lactamases except OXA-9 and OXA-12 (45 and 42% amino acid identity, respectively). OXA-18 is likely to be chromosomally encoded since no plasmid was found in the strain and because attempts to transfer the resistance marker failed. OXA-18 is peculiar since it is a class D beta-lactamase which confers high resistance to extended-spectrum cephalosporins and seems to have unique hydrolytic properties among non-class A enzymes.

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OXA-18, a class D clavulanic acid-inhibited extended-spectrum beta-lactamase from Pseudomonas aeruginosa.
L N Philippon, T Naas, A T Bouthors, V Barakett, P Nordmann
Antimicrobial Agents and Chemotherapy Oct 1997, 41 (10) 2188-2195; DOI: 10.1128/AAC.41.10.2188

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OXA-18, a class D clavulanic acid-inhibited extended-spectrum beta-lactamase from Pseudomonas aeruginosa.
L N Philippon, T Naas, A T Bouthors, V Barakett, P Nordmann
Antimicrobial Agents and Chemotherapy Oct 1997, 41 (10) 2188-2195; DOI: 10.1128/AAC.41.10.2188
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