Novel Carbapenem-Hydrolyzing Oxacillinase OXA-62 from Pandoraea pnomenusa

Author:

Schneider Ines1,Queenan Anne Marie2,Bauernfeind Adolf1

Affiliation:

1. MICOER Institute, Munich, Germany

2. Johnson & Johnson Pharmaceutical Research and Development, Raritan, New Jersey

Abstract

ABSTRACT Pandoraea spp. are gram-negative, glucose nonfermenting rods detectable in blood cultures and sputa of cystic fibrosis patients. They are resistant to various antibiotic groups, with imipenem being the only active β-lactam. We isolated an imipenem-resistant (MIC, 64 μg/ml) Pandoraea pnomenusa strain from a cystic fibrosis patient. Cloning and sequencing identified two β-lactamases of Bush group 2d, namely, the known OXA-33, located on an integron, and the novel carbapenem-hydrolyzing oxacillinase OXA-62. OXA-62 is only distantly related to other oxacillinases (OXA-50 being closest with 43% amino acid identity). It hydrolyzes penicillins, oxacillin, imipenem, and meropenem but not expanded-spectrum cephalosporins. The bla OXA-62 gene is chromosome located. No transposable elements were found in its genetic neighborhood. With OXA-62-specific primers, bla OXA-62 could be identified in all P. pnomenusa strains and appears to be species specific. This additional mechanism of carbapenem resistance further complicates the treatment of infections caused by P. pnomenusa .

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

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