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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2009-1-12
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pubmed:abstractText |
The role of clinically important multidrug resistance (MDR) efflux pumps in bacterial resistance to various human antimicrobial peptides (AMPs), including cathelicidin LL-37, the alpha-defensins human neutrophil peptides (HNPs)-1-3 and HD-5 and the beta-defensins hBD-2 and -3, was investigated. AMP susceptibility testing was performed by killing assays and standard minimal inhibitory concentration assays. AMP susceptibility was determined in Escherichia coli and Pseudomonas aeruginosa strains overexpressing resistance-nodulation-cell division (RND)-type pumps AcrAB and MexAB, respectively, and in their pump-deficient parental strains. Furthermore, the impact of a member of the major facilitator (MF) efflux pump family was investigated in Staphylococcus aureus overexpressing NorA and in wild-type strains. The E. coli AcrAB and P. aeruginosa MexAB RND-type efflux pumps as well as the S. aureus NorA MF efflux pump were unable to confer resistance to AMPs. These findings do not support a critical role of MDR efflux pumps in the tested pathogens as a strategy to increase virulence by circumventing the antimicrobial action of innate defence AMPs.
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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/AcrA protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Antimicrobial Cationic Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MexA protein, Pseudomonas aeruginosa,
http://linkedlifedata.com/resource/pubmed/chemical/MexB protein, Pseudomonas aeruginosa,
http://linkedlifedata.com/resource/pubmed/chemical/Multidrug Resistance-Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/NorA protein, Staphylococcus
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0924-8579
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
33
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
174-6
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pubmed:meshHeading |
pubmed-meshheading:18945595-Antimicrobial Cationic Peptides,
pubmed-meshheading:18945595-Bacterial Outer Membrane Proteins,
pubmed-meshheading:18945595-Bacterial Proteins,
pubmed-meshheading:18945595-Drug Resistance, Bacterial,
pubmed-meshheading:18945595-Escherichia coli,
pubmed-meshheading:18945595-Escherichia coli Proteins,
pubmed-meshheading:18945595-Gene Deletion,
pubmed-meshheading:18945595-Gene Dosage,
pubmed-meshheading:18945595-Humans,
pubmed-meshheading:18945595-Lipoproteins,
pubmed-meshheading:18945595-Membrane Transport Proteins,
pubmed-meshheading:18945595-Microbial Sensitivity Tests,
pubmed-meshheading:18945595-Microbial Viability,
pubmed-meshheading:18945595-Multidrug Resistance-Associated Proteins,
pubmed-meshheading:18945595-Pseudomonas aeruginosa,
pubmed-meshheading:18945595-Staphylococcus aureus
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pubmed:year |
2009
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pubmed:articleTitle |
Resistance against antimicrobial peptides is independent of Escherichia coli AcrAB, Pseudomonas aeruginosa MexAB and Staphylococcus aureus NorA efflux pumps.
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pubmed:affiliation |
Center for Infectious Diseases and Travel Medicine, Department of Medicine, University Hospital, Freiburg, Germany. siegbert.rieg@uniklinik-freiburg.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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