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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2001-6-29
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pubmed:abstractText |
Bacterial lipoproteins (BLP) trigger immune responses via Toll-like receptor 2 (TLR2) and their immunostimulatory properties are attributed to the presence of a lipoylated N-terminus. Most BLP are triacylated at the N-terminus cysteine residue, but mycoplasmal macrophage-activating lipopeptide-2 kD (MALP-2) is only diacylated. Here we show that TLR6-deficient (TLR6(-/-)) cells are unresponsive to MALP-2 but retain their normal responses to lipopeptides of other bacterial origins. Reconstitution experiments in TLR2(-/-) TLR6(-/-) embryonic fibroblasts reveal that co-expression of TLR2 and TLR6 is absolutely required for MALP-2 responsiveness. Taken together, these results show that TLR6 recognizes MALP-2 cooperatively with TLR2, and appears to discriminate between the N-terminal lipoylated structures of MALP-2 and lipopeptides derived from other bacteria.
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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/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-12,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-6,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/TLR2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/TLR6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tlr6 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptor 6,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptors,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/macrophage stimulatory lipopeptide 2
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0953-8178
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
933-40
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11431423-Animals,
pubmed-meshheading:11431423-Bacterial Proteins,
pubmed-meshheading:11431423-Cells, Cultured,
pubmed-meshheading:11431423-Drosophila Proteins,
pubmed-meshheading:11431423-Humans,
pubmed-meshheading:11431423-Interleukin-12,
pubmed-meshheading:11431423-Interleukin-6,
pubmed-meshheading:11431423-Lipopeptides,
pubmed-meshheading:11431423-Lipoproteins,
pubmed-meshheading:11431423-Macrophages, Peritoneal,
pubmed-meshheading:11431423-Membrane Glycoproteins,
pubmed-meshheading:11431423-Mice,
pubmed-meshheading:11431423-Mice, Inbred A,
pubmed-meshheading:11431423-Mice, Inbred C57BL,
pubmed-meshheading:11431423-Mice, Knockout,
pubmed-meshheading:11431423-NF-kappa B,
pubmed-meshheading:11431423-Nitric Oxide,
pubmed-meshheading:11431423-Oligopeptides,
pubmed-meshheading:11431423-Receptors, Cell Surface,
pubmed-meshheading:11431423-Signal Transduction,
pubmed-meshheading:11431423-Toll-Like Receptor 2,
pubmed-meshheading:11431423-Toll-Like Receptor 6,
pubmed-meshheading:11431423-Toll-Like Receptors,
pubmed-meshheading:11431423-Tumor Necrosis Factor-alpha
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pubmed:year |
2001
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pubmed:articleTitle |
Discrimination of bacterial lipoproteins by Toll-like receptor 6.
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pubmed:affiliation |
Department of Host Defense, Research Institute for Microbial Diseases, Osaka University, Suita, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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