pubmed-article:14733728 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14733728 | lifeskim:mentions | umls-concept:C0033809 | lld:lifeskim |
pubmed-article:14733728 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
pubmed-article:14733728 | lifeskim:mentions | umls-concept:C0023767 | lld:lifeskim |
pubmed-article:14733728 | lifeskim:mentions | umls-concept:C1411976 | lld:lifeskim |
pubmed-article:14733728 | lifeskim:mentions | umls-concept:C1880371 | lld:lifeskim |
pubmed-article:14733728 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:14733728 | pubmed:dateCreated | 2004-1-21 | lld:pubmed |
pubmed-article:14733728 | pubmed:abstractText | Lipid A is the pro-inflammatory component of bacterial lipopolysaccharide, the major surface component of Gram-negative bacteria. Gram-negative bacteria alter the structure of lipid A in response to specific environmental conditions including those found upon colonization of a host. The opportunistic pathogen Pseudomonas aeruginosa synthesizes a unique hexa-acylated lipid A containing palmitate and aminoarabinose during adaptation to the cystic fibrosis airway. Different lipid A species are observed in P. aeruginosa isolated from non-cystic fibrosis associated infections. Here we report that P. aeruginosa isolates from the airway of a cystic fibrosis patient with severe pulmonary disease synthesized a novel hepta-acylated lipid A. Cystic fibrosis-specific P. aeruginosa lipid A modifications result in resistance to host antimicrobial peptides and increased recognition by human Toll-like receptor 4 (TLR4). Using P. aeruginosa lipid A with different levels of acylation, we identified a 222 amino acid region in the extracellular portion of human TLR4 that is required for the differential recognition of cystic fibrosis-specific lipid A. P. aeruginosa adaptation to the human airway may, therefore, play a fundamental role in the progressive lung damage associated with cystic fibrosis. | lld:pubmed |
pubmed-article:14733728 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14733728 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14733728 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14733728 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14733728 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14733728 | pubmed:language | eng | lld:pubmed |
pubmed-article:14733728 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14733728 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14733728 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14733728 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14733728 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14733728 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14733728 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14733728 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14733728 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14733728 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14733728 | pubmed:issn | 0968-0519 | lld:pubmed |
pubmed-article:14733728 | pubmed:author | pubmed-author:WilsonChristo... | lld:pubmed |
pubmed-article:14733728 | pubmed:author | pubmed-author:MillerSamuel... | lld:pubmed |
pubmed-article:14733728 | pubmed:author | pubmed-author:HajjarAdeline... | lld:pubmed |
pubmed-article:14733728 | pubmed:author | pubmed-author:ErnstRobert... | lld:pubmed |
pubmed-article:14733728 | pubmed:author | pubmed-author:TsaiJeff HJH | lld:pubmed |
pubmed-article:14733728 | pubmed:author | pubmed-author:MoskowitzSamu... | lld:pubmed |
pubmed-article:14733728 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14733728 | pubmed:volume | 9 | lld:pubmed |
pubmed-article:14733728 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14733728 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14733728 | pubmed:pagination | 395-400 | lld:pubmed |
pubmed-article:14733728 | pubmed:dateRevised | 2011-5-5 | lld:pubmed |
pubmed-article:14733728 | pubmed:meshHeading | pubmed-meshheading:14733728... | lld:pubmed |
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pubmed-article:14733728 | pubmed:meshHeading | pubmed-meshheading:14733728... | lld:pubmed |
pubmed-article:14733728 | pubmed:meshHeading | pubmed-meshheading:14733728... | lld:pubmed |
pubmed-article:14733728 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:14733728 | pubmed:articleTitle | Pseudomonas aeruginosa lipid A diversity and its recognition by Toll-like receptor 4. | lld:pubmed |
pubmed-article:14733728 | pubmed:affiliation | Department of Medicine, HSB K-155, Box 357710, University of Washington, Seattle, WA 98195, USA. rkernst@u.washington.edu | lld:pubmed |
pubmed-article:14733728 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:14733728 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:14733728 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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