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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2002-5-24
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pubmed:abstractText |
Listeriolysin O (LLO) is a pore-forming cytolysin secreted by the pathogen Listeria monocytogenes and is required for its intracellular survival. We recently demonstrated that in endothelial cells, LLO activates the NF-kappaB signalling pathway. In this work, we studied the LLO-induced molecular cascade of NF-kappaB activation with a cellular model extensively used to analyse the signalling pathway of NF-kappaB activation, i.e. the human embryonic kidney HEK-293 cell line and its derivatives (transfectants or mutants). When the stably transfected derivative HEK-293 cells expressing IL-1RI were exposed to LLO, a strong NF-kappaB activation was detected, contrasting with other cell lines (HEK-293 wild type, HEK-293.T and COS) expressing a very low level of IL-1RI. Although a delayed kinetics of LLO-dependent NF-kappaB activation suggests an autocrine or paracrine IL-1-dependent pathway, we found that LLO-dependent NF-kappaB activation did not require the IL-1 protein synthesis nor the interaction with the IL-1RI specific receptor. Herein, we demonstrated that LLO-dependent NF-kappaB activation requires the activation of the IkappaB kinase beta (IKKbeta) subunit of IKK complex to phosphorylate and degrade cytoplasmic IkappaBalpha, a natural inhibitor of NF-kappaB. The activation induced by LLO does not require the adapters MyD88 and IL-1R-associated kinase (IRAK). We suggested that LLO induces a distinct signalling pathway from that of IL-1 and its receptor.
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/CHUK protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cycloheximide,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hemolysin Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/I-kappa B Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/IKBKB protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/IKBKE protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/MYD88 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Myeloid Differentiation Factor 88,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Synthesis Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/hlyA protein, Listeria monocytogenes
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0950-382X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1407-19
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12028384-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:12028384-Animals,
pubmed-meshheading:12028384-Antigens, Differentiation,
pubmed-meshheading:12028384-Bacterial Proteins,
pubmed-meshheading:12028384-Bacterial Toxins,
pubmed-meshheading:12028384-Cell Line,
pubmed-meshheading:12028384-Cycloheximide,
pubmed-meshheading:12028384-Flow Cytometry,
pubmed-meshheading:12028384-Genes, Reporter,
pubmed-meshheading:12028384-Heat-Shock Proteins,
pubmed-meshheading:12028384-Hemolysin Proteins,
pubmed-meshheading:12028384-Humans,
pubmed-meshheading:12028384-I-kappa B Kinase,
pubmed-meshheading:12028384-Interleukin-1,
pubmed-meshheading:12028384-Listeria monocytogenes,
pubmed-meshheading:12028384-Myeloid Differentiation Factor 88,
pubmed-meshheading:12028384-NF-kappa B,
pubmed-meshheading:12028384-Protein Synthesis Inhibitors,
pubmed-meshheading:12028384-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12028384-Receptors, Immunologic,
pubmed-meshheading:12028384-Signal Transduction
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pubmed:year |
2002
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pubmed:articleTitle |
Listeriolysin O secreted by Listeria monocytogenes induces NF-kappaB signalling by activating the IkappaB kinase complex.
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pubmed:affiliation |
Laboratoire de Microbiologie, INSERM U-411, Faculté de Médecine Necker, 75730 Paris Cedex 15, France. kayal@necker.fr
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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