OXA-163, an OXA-48-Related Class D β-Lactamase with Extended Activity Toward Expanded-Spectrum Cephalosporins

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Detection of OXA-370, an OXA-48-related class D β-lactamase, in Enterobacter hormaechei from Brazil.

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Noncarbapenemase OXA-48 Variants (OXA-163 and OXA-405) Falsely Detected as Carbapenemases by the β Carba Test.

Laurent Dortet, Thierry Naas Associated French National Reference Center for Antibiotic Resistance, Le Kremlin-Bicêtre, France; Research Unit EA7361 “Structure, Dynamic, Function and Expression of Broad Spectrum β-Lactamases,” Faculty of Medicine, University Paris-Sud, Le Kremlin-Bicêtre, France; Department of Bacteriology-Parasitology-Hygiene, Bicêtre Hospital, Assistance Publique—Hôpitaux de ...

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

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 pr...

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Structures of the class D Carbapenemases OXA-23 and OXA-146: mechanistic basis of activity against carbapenems, extended-spectrum cephalosporins, and aztreonam.

Class D β-lactamases that hydrolyze carbapenems such as imipenem and doripenem are a recognized danger to the efficacy of these "last-resort" β-lactam antibiotics. Like all known class D carbapenemases, OXA-23 cannot hydrolyze the expanded-spectrum cephalosporin ceftazidime. OXA-146 is an OXA-23 subfamily clinical variant that differs from the parent enzyme by a single alanine (A220) inserted i...

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OXA-17, a further extended-spectrum variant of OXA-10 beta-lactamase, isolated from Pseudomonas aeruginosa.

Pseudomonas aeruginosa isolates 871 and 873 were isolated at Hacettepe University Hospital in Ankara and were highly resistant to ceftazidime (MIC, 128 microg/ml). Each produced three beta-lactamases, with pIs of 5.3, 6.1, and 7.9. The beta-lactamase with a pI of 5.3 was previously shown to be PER-1 enzyme. The antibiograms of the isolates were not entirely explained by production of PER-1 enzy...

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ژورنال

عنوان ژورنال: Antimicrobial Agents and Chemotherapy

سال: 2011

ISSN: 0066-4804,1098-6596

DOI: 10.1128/aac.00022-11