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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2003-10-9
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pubmed:abstractText |
An isolate of Pseudomonas aeruginosa from cystic fibrosis was highly resistant to beta-lactams and beta-lactamase inhibitors. The resistant determinants of clinical isolate to imipenem, ceftazidim, cefriaxone and cefepime were conjugally nontransferable. The slow or nonenzymically mediated breakdown of imipenem and other broad-spectrum beta-lactams suggested the resistance of P. aeruginosa isolate to these drugs which may be attributed to both permeability and efflux. Impaired penetration of imipenem and other beta-lactams through the membrane was detected by a diminished expression of outer-membrane proteins of approximate molar mass of 46 and 39 kDa, matched to OprD and OprF, respectively. Efflux resistance mechanism for meropenem and beta-lactams has been ruled out since the isolate failed to express outer-membrane protein of approximately 50 kDa which is matched to the OprM protein channel. Thus, reduced permeability in the clinical isolate is the main mechanism conferring resistance against beta-lactams including imipenem.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ceftazidime,
http://linkedlifedata.com/resource/pubmed/chemical/Ceftriaxone,
http://linkedlifedata.com/resource/pubmed/chemical/Cephalosporins,
http://linkedlifedata.com/resource/pubmed/chemical/Imipenem,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/OprD protein, Pseudomonas aeruginosa,
http://linkedlifedata.com/resource/pubmed/chemical/OprM protein, Pseudomonas aeruginosa,
http://linkedlifedata.com/resource/pubmed/chemical/Porins,
http://linkedlifedata.com/resource/pubmed/chemical/cefepime
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pubmed:status |
MEDLINE
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pubmed:issn |
0015-5632
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
48
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
529-33
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pubmed:dateRevised |
2006-8-31
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pubmed:meshHeading |
pubmed-meshheading:14533486-Anti-Bacterial Agents,
pubmed-meshheading:14533486-Bacterial Outer Membrane Proteins,
pubmed-meshheading:14533486-Biological Transport, Active,
pubmed-meshheading:14533486-Ceftazidime,
pubmed-meshheading:14533486-Ceftriaxone,
pubmed-meshheading:14533486-Cell Membrane Permeability,
pubmed-meshheading:14533486-Cephalosporins,
pubmed-meshheading:14533486-Conjugation, Genetic,
pubmed-meshheading:14533486-Cystic Fibrosis,
pubmed-meshheading:14533486-Drug Resistance, Multiple, Bacterial,
pubmed-meshheading:14533486-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:14533486-Genes, Bacterial,
pubmed-meshheading:14533486-Humans,
pubmed-meshheading:14533486-Imipenem,
pubmed-meshheading:14533486-Membrane Transport Proteins,
pubmed-meshheading:14533486-Microbial Sensitivity Tests,
pubmed-meshheading:14533486-Porins,
pubmed-meshheading:14533486-Pseudomonas aeruginosa
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pubmed:year |
2003
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pubmed:articleTitle |
Lack of efflux mechanism in a clinical isolate of Pseudomonas aeruginosa highly resistant to beta-lactams and imipenem.
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pubmed:affiliation |
Microbiology Division, Faculty of Pharmacy, King Saud University, Riyadh, Saudi Arabia. akadry@ksu.edu.sa
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pubmed:publicationType |
Journal Article
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