Source:http://linkedlifedata.com/resource/pubmed/id/19573161
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
11
|
| pubmed:dateCreated |
2009-10-14
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| pubmed:abstractText |
The intracellular pathogen Legionella pneumophila activates the transcription factor NF-kappaB in macrophages and human epithelial cells, contributing to cytokine production and anti-apoptosis. The former is important for the innate immune response to infection, the latter for intracellular replication by securing host cell survival. Here, we demonstrate biphasic activation of NF-kappaB by L. pneumophila in human epithelial cells, using a p65-GFP expressing variant of A549 cells. Early in infection, a strong but transient nuclear translocation of p65 was observed. Only flagellin-deficient (DeltafliA and DeltaflaA) mutants could not induce this first, TLR5 and MyD88-dependent activation. The second p65 translocation event, however, is a long-term activation, independent of flagellin, TLR5 and MyD88, and marked by permanent nuclear localization of p65-GFP without oscillation for 30 h. Persistent p65 translocation also involved degradation of IkappaBalpha and upregulation of anti-apoptotic genes. L. pneumophila mutants lacking a functional Dot/Icm secretion system (DeltadotA; DeltaicmB/dotO), Dot/Icm effectors (DeltasdbA; DeltalubX) and two bacterial effector mutants (DeltaenhC; DeltaptsP) could not induce persistent p65 translocation. Strikingly, all these mutants were deficient in intracellular replication in A549 cells. Our data underline the strong connection between NF-kappaB activation and intracellular replication and hints at an active interference of NF-kappaB signalling by L. pneumophila.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Flagellin,
http://linkedlifedata.com/resource/pubmed/chemical/I-kappa B Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappaB inhibitor alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/TIRAP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/TLR5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptor 5,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor RelA,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
1462-5822
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:volume |
11
|
| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1638-51
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| pubmed:meshHeading |
pubmed-meshheading:19573161-Bacterial Proteins,
pubmed-meshheading:19573161-Cell Line,
pubmed-meshheading:19573161-Cell Nucleus,
pubmed-meshheading:19573161-Epithelial Cells,
pubmed-meshheading:19573161-Flagellin,
pubmed-meshheading:19573161-Gene Deletion,
pubmed-meshheading:19573161-Humans,
pubmed-meshheading:19573161-I-kappa B Proteins,
pubmed-meshheading:19573161-Legionella pneumophila,
pubmed-meshheading:19573161-Membrane Glycoproteins,
pubmed-meshheading:19573161-NF-kappa B,
pubmed-meshheading:19573161-Receptors, Interleukin-1,
pubmed-meshheading:19573161-Toll-Like Receptor 5,
pubmed-meshheading:19573161-Transcription Factor RelA,
pubmed-meshheading:19573161-Virulence Factors
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| pubmed:year |
2009
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| pubmed:articleTitle |
Temporal resolution of two-tracked NF-kappaB activation by Legionella pneumophila.
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| pubmed:affiliation |
Max Planck Institute for Infection Biology, Department of Molecular Biology, Berlin, Germany.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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