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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2016.1
- 수록면
- 611 - 613 (3page)
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초록· 키워드
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Dear Editor, Multidrug resistance of Pseudomonas aeruginosa has been attributed to both intrinsic and acquired antibiotic-resistance mechanisms. Multidrug-resistant (MDR) P. aeruginosa isolates have become a serious healthcare problem worldwide because they are resistant to almost all β-lactams, aminoglycosides, and quinolones. Production of zinc-dependent metallo-β-lactamases (MBLs) has been identified as the most significant mechanism among carbapenem-resistant P. aeruginosa isolates [1]. MBLs are of particular clinical concern because of their broad-spectrum activities, and Imipenemase (IMP)-, Verona Integron-Encoded Metallo-β-lactamase (VIM)-, Sao Paulo metallo-β-lactamase (SPM)-, Germany imipenemase (GIM)-, and New Delhi Metallo-β-lactamase (NDM)-type MBLs have been identified in P. aeruginosa worldwide [2]. Forty-six variants of VIM enzymes have been identified to date (http://www.lahey.org/Studies/other.asp). VIM-38 was recently identified in P. aeruginosa isolates in Turkey and was shown to differ from VIM-5 by a single substitution (Ala316Val) [3]. In P. aeruginosa, VIM-type MBLs have been reported within mobile genetic elements such as integrons, which contribute to the dissemination of antibiotic resistance [3].
We here report a new clinical P. aeruginosa strain isolated from a blood sample on January 2015 at Rize State Hospital in Turkey and identified by using the API 32GN system (bioMerieux, Marcy-l’Etoile, France). Minimal inhibitory concentrations were determined on a VITEK system for the following antibiotics: piperacillin/tazobactam, ceftazidime, cefepime, amikacin, netilmicin, ciprofloxacin, levofloxacin, imipenem, meropenem, cefoperazone-sulbactam, and inducible β-lactamase. 16S rDNA sequencing was used for molecular identification, performed according to Cicek et al [4].
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참고문헌 (10)
참고문헌 신청
Cornaglia G / 2011 / Metallo-β-lactamases: a last frontier for β-lactams? / Lancet Infect Dis 11:381~393
Bebrone C / 2007 / Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily / Biochem Pharmacol 74:1686~1701
Iraz M / 2014 / Characterization of novel VIM carbapenemase, VIM-38, and first detection of GES-5 carbapenem-hydrolyzing β-lactamases in Pseudomonas aeruginosa in Turkey / Microbiol Infect Dis 78:292~294
Cicek AC / 2014 / Determination of a novel integron-located variant (blaOXA-320) of Class D β-lactamase in Proteus mirabilis / J Basic Microbiol 54:1030~1035
Meryem Iraz / 2015 / Distribution of β-Lactamase Genes Among Carbapenem-Resistant Klebsiella pneumoniae Strains Isolated From Patients in Turkey / Annals of Laboratory Medicine 35(6):595~601
Bebrone C / 2007 / Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily / Biochem Pharmacol 74:1686~1701
Iraz M / 2014 / Characterization of novel VIM carbapenemase, VIM-38, and first detection of GES-5 carbapenem-hydrolyzing β-lactamases in Pseudomonas aeruginosa in Turkey / Microbiol Infect Dis 78:292~294
Cicek AC / 2014 / Determination of a novel integron-located variant (blaOXA-320) of Class D β-lactamase in Proteus mirabilis / J Basic Microbiol 54:1030~1035
Meryem Iraz / 2015 / Distribution of β-Lactamase Genes Among Carbapenem-Resistant Klebsiella pneumoniae Strains Isolated From Patients in Turkey / Annals of Laboratory Medicine 35(6):595~601
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