| pubmed-article:11912497 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11912497 | lifeskim:mentions | umls-concept:C2697656 | lld:lifeskim |
| pubmed-article:11912497 | lifeskim:mentions | umls-concept:C0175697 | lld:lifeskim |
| pubmed-article:11912497 | lifeskim:mentions | umls-concept:C1321919 | lld:lifeskim |
| pubmed-article:11912497 | lifeskim:mentions | umls-concept:C0023810 | lld:lifeskim |
| pubmed-article:11912497 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:11912497 | lifeskim:mentions | umls-concept:C1554963 | lld:lifeskim |
| pubmed-article:11912497 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:11912497 | pubmed:dateCreated | 2002-3-28 | lld:pubmed |
| pubmed-article:11912497 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11912497 | pubmed:abstractText | Lipopolysaccharide (LPS) is the principal proinflammatory component of the Gram-negative bacterial envelope and is recognized by the Toll-like receptor 4 (TLR4)-MD-2 receptor complex. Bacteria can alter the acylation state of their LPS in response to environmental changes. One opportunistic bacterium, Pseudomonas aeruginosa, synthesizes more highly acylated (hexa-acylated) LPS structures during adaptation to the cystic fibrosis airway. Here we show that human, but not murine, TLR4-MD-2 recognizes this adaptation and transmits robust proinflammatory signals in response to hexa-acylated but not penta-acylated LPS from P. aeruginosa. Whereas responses to lipidIVA and taxol are dependent on murine MD-2, discrimination of P. aeruginosa LPS structures is mediated by an 82-amino-acid region of human TLR4 that is hypervariable across species. Thus, in contrast to mice, humans use TLR4 to recognize a molecular signature of bacterial-host adaptation to modulate the innate immune response. | lld:pubmed |
| pubmed-article:11912497 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11912497 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11912497 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11912497 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11912497 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11912497 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11912497 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11912497 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11912497 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11912497 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11912497 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11912497 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11912497 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:11912497 | pubmed:issn | 1529-2908 | lld:pubmed |
| pubmed-article:11912497 | pubmed:author | pubmed-author:WilsonChristo... | lld:pubmed |
| pubmed-article:11912497 | pubmed:author | pubmed-author:MillerSamuel... | lld:pubmed |
| pubmed-article:11912497 | pubmed:author | pubmed-author:HajjarAdeline... | lld:pubmed |
| pubmed-article:11912497 | pubmed:author | pubmed-author:ErnstRobert... | lld:pubmed |
| pubmed-article:11912497 | pubmed:author | pubmed-author:TsaiJeff HJH | lld:pubmed |
| pubmed-article:11912497 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11912497 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:11912497 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11912497 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11912497 | pubmed:pagination | 354-9 | lld:pubmed |
| pubmed-article:11912497 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:11912497 | pubmed:meshHeading | pubmed-meshheading:11912497... | lld:pubmed |
| pubmed-article:11912497 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11912497 | pubmed:articleTitle | Human Toll-like receptor 4 recognizes host-specific LPS modifications. | lld:pubmed |
| pubmed-article:11912497 | pubmed:affiliation | Department of Immunology, University of Washington, Seattle, WA 98195, USA. | lld:pubmed |
| pubmed-article:11912497 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11912497 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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