4.7 Article

PME-1, an Extended-Spectrum β-Lactamase Identified in Pseudomonas aeruginosa

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ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
卷 55, 期 6, 页码 2710-2713

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AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.01660-10

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  1. National Institutes of Health [1K22AI080584, 1R03AI079296]
  2. China Scholarship Council (CSC)
  3. Pennsylvania Department of Health [4100047864]

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A novel extended-spectrum beta-lactamase (ESBL) was identified in a Pseudomonas aeruginosa clinical isolate obtained from a patient admitted to a hospital in Pennsylvania in 2008. The patient had a prolonged hospitalization in a hospital in Dubai, United Arab Emirates, before being transferred to the United States. The novel ESBL, designated PME-1 (Pseudomonas aeruginosa ESBL 1), is a molecular class A, Bush-Jacoby-Medeiros group 2be enzyme and shared 50, 43, and 41% amino acid identity with the L2 beta-lactamase of Stenotrophomonas maltophilia, CTX-M-9, and KPC-2, respectively. PME-1 conferred clinically relevant resistance to ceftazidime, cefotaxime, cefepime, and aztreonam in P. aeruginosa PAO1 but not to carbapenems. Purified PME-1 showed good hydrolytic activity against ceftazidime, cefotaxime, and aztreonam, while activity against carbapenems and cefepime could not be measured. PME-1 was inhibited well by beta-lactamase inhibitors, including clavulanic acid, sulbactam, and tazobactam. The bla(PME-1) gene was carried by an approximately 9-kb plasmid and flanked by tandem ISCR24 elements.

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