Source:http://linkedlifedata.com/resource/pubmed/id/16920954
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2006-8-21
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pubmed:abstractText |
Lipoteichoic acid (LTA) derived from Staphylococcus aureus is reported to be a ligand of TLR2. However, we previously demonstrated that LTA fraction prepared from bacterial cells contains lipoproteins, which activate cells via TLR2. In this study, we investigated the immunobiological activity of LTA fraction obtained from S. aureus wild-type strain, lipoprotein diacylglycerol transferase deletion (delta lgt) mutant, which lacks palmitate-labeled lipoproteins, and its complemented strain and evaluated the activity of LTA molecule. LTA fraction was prepared by butanol extraction of the bacteria followed by hydrophobic interaction chromatography. Although all LTA fractions activated cells through TLR2, the LTA from delta lgt mutant was 100-fold less potent than those of wild-type and complemented strains. However, no significant structural difference in LTA was observed in NMR spectra. Further, alanylation of LTA molecule showed no effect in immunobiological activity. These results showed that not LTA molecule but lipoproteins are dominant immunobiologically active TLR2 ligand in S. aureus.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Teichoic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Tlr2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/lipoteichoic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
177
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3162-9
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:16920954-Acyltransferases,
pubmed-meshheading:16920954-Animals,
pubmed-meshheading:16920954-Cell Line,
pubmed-meshheading:16920954-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:16920954-Lipopolysaccharides,
pubmed-meshheading:16920954-Lipoproteins,
pubmed-meshheading:16920954-Mice,
pubmed-meshheading:16920954-Mutation,
pubmed-meshheading:16920954-NF-kappa B,
pubmed-meshheading:16920954-Staphylococcus aureus,
pubmed-meshheading:16920954-Teichoic Acids,
pubmed-meshheading:16920954-Toll-Like Receptor 2,
pubmed-meshheading:16920954-Tumor Necrosis Factor-alpha
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pubmed:year |
2006
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pubmed:articleTitle |
Not lipoteichoic acid but lipoproteins appear to be the dominant immunobiologically active compounds in Staphylococcus aureus.
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pubmed:affiliation |
Department of Nanostructure and Advanced Materials, Kagoshima University, Kagoshima, Japan. hassy@eng.kagoshima-u.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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