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Functional and Structural Characterization of OXA-935, a Novel OXA-10-Family β-Lactamase from Pseudomonas aeruginosa

Authors :
Nathan B. Pincus
Monica Rosas-Lemus
Samuel W. M. Gatesy
Hanna K. Bertucci
Joseph S. Brunzelle
George Minasov
Ludmilla A. Shuvalova
Marine Lebrun-Corbin
Karla J. F. Satchell
Egon A. Ozer
Alan R. Hauser
Kelly E. R. Bachta
Source :
Antimicrobial agents and chemotherapy. 66(10)
Publication Year :
2022

Abstract

Resistance to antipseudomonal penicillins and cephalosporins is often driven by the overproduction of the intrinsic β-lactamase AmpC. However, OXA-10-family β-lactamases are a rich source of resistance in Pseudomonas aeruginosa. OXA β-lactamases have a propensity for mutation that leads to extended spectrum cephalosporinase and carbapenemase activity. In this study, we identified isolates from a subclade of the multidrug-resistant (MDR) high risk P. aeruginosa clonal complex CC446 with a resistance to ceftazidime. A genomic analysis revealed that these isolates harbored a plasmid containing a novel allele of

Details

ISSN :
10986596
Volume :
66
Issue :
10
Database :
OpenAIRE
Journal :
Antimicrobial agents and chemotherapy
Accession number :
edsair.doi.dedup.....5825bc1a60be79982c187a56d96e60f3