Beta-lactamase Enzymes of Clinical Pseudomonas aeruginosa Strains
dc.contributor.author | Pasa, O. | |
dc.contributor.author | Ozer, B. | |
dc.contributor.author | Duran, N. | |
dc.contributor.author | Inci, M. | |
dc.contributor.author | Yula, E. | |
dc.date.accessioned | 2024-09-18T19:54:17Z | |
dc.date.available | 2024-09-18T19:54:17Z | |
dc.date.issued | 2016 | |
dc.department | Hatay Mustafa Kemal Üniversitesi | en_US |
dc.description.abstract | Objectives: In this study, the production of extended spectrum beta-lactamase (ESBL), metallo-betalacatamase (MBL) and AmpC beta-lactamase enzymes of Pseudomonas aeruginosa (P aeruginosa) strains which were isolated from clinical samples were investigated. AmpC gene was also detected by the polymerase chain reaction (PCR) analysis. Methods: A hundred strains of P aeruginosa were included in the study. The presence of ESBL was investigated with combined disk confirmation test, MBL was investigated with E-test method and AmpC beta-lactamase was investigated with disk induction test. In order to detect the production of AmpC beta-lactamase genotypically, the PCR method was used. Results: Only one strain was found to be MBL positive. Four per cent of strains were found to be ESBL positive. AmpC beta-lactamase production was positive in 73% of the strains with disk induction test. AmpC gene was detected in 96% of the studied strains with the PCR method. Conclusion: While ESBL and MBL rates in this study were significantly lower than those found in other studies, the rate of AmpC beta-lactamase was higher. Although AmpC gene was detected in some strains (23%), they were not found to produce AmpC beta-lactamase with disk induction test. | en_US |
dc.description.sponsorship | Mustafa Kemal University Scientific Research Projects [BAP 1204 U 0106] | en_US |
dc.description.sponsorship | This study was granted by Mustafa Kemal University Scientific Research Projects (BAP 1204 U 0106) and presented in the 2nd National Congress of Clinical Microbiology in 2013 in Turkey. | en_US |
dc.identifier.doi | 10.7727/wimj.2014.362 | |
dc.identifier.endpage | 45 | en_US |
dc.identifier.issn | 0043-3144 | |
dc.identifier.issue | 1 | en_US |
dc.identifier.pmid | 26901598 | en_US |
dc.identifier.startpage | 40 | en_US |
dc.identifier.uri | https://doi.org/10.7727/wimj.2014.362 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12483/7625 | |
dc.identifier.volume | 65 | en_US |
dc.identifier.wos | WOS:000393480700007 | en_US |
dc.identifier.wosquality | Q4 | en_US |
dc.indekslendigikaynak | Web of Science | en_US |
dc.indekslendigikaynak | PubMed | en_US |
dc.language.iso | en | en_US |
dc.publisher | Univ West Indies Faculty Medical Sciences | en_US |
dc.relation.ispartof | West Indian Medical Journal | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.rights | info:eu-repo/semantics/openAccess | en_US |
dc.subject | AmpC beta-lactamase | en_US |
dc.subject | AmpC gene | en_US |
dc.subject | extended spectrum beta-lactamase | en_US |
dc.subject | metallo-beta-lactamase | en_US |
dc.subject | Pseudomonas aeruginosa | en_US |
dc.subject | resistance | en_US |
dc.title | Beta-lactamase Enzymes of Clinical Pseudomonas aeruginosa Strains | en_US |
dc.type | Article | en_US |
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