| pubmed-article:15014080 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15014080 | lifeskim:mentions | umls-concept:C0036126 | lld:lifeskim |
| pubmed-article:15014080 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:15014080 | lifeskim:mentions | umls-concept:C0023767 | lld:lifeskim |
| pubmed-article:15014080 | lifeskim:mentions | umls-concept:C1411976 | lld:lifeskim |
| pubmed-article:15014080 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:15014080 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:15014080 | pubmed:dateCreated | 2004-5-4 | lld:pubmed |
| pubmed-article:15014080 | pubmed:abstractText | Toll-like receptor 4 (TLR4)-mediated responses, which are induced by the lipid A portion of lipopolysaccharide, are important for host defense against Salmonellae infection. A variety of different data indicate that the acylation state of lipid A can alter TLR4-mediated responses. The S. typhimurium virulence gene product PhoP/PhoQ signals the presence of host microenvironments to regulate the expression of a lipid A 3-O-deacylase, PagL, and a lipid A palmitoyltransferase, PagP. We now demonstrate that 3-O-deacylation and palmitoylation of lipid A decreases its ability to induce TLR4-mediated signaling. Deacylated lipid A, deacylated and palmitoylated lipid A, palmitoylated lipid A, and unmodified lipid A species were purified from Escherichia coli heterologously expressing PagL and/or PagP. The purified lipid A preparations showed spectra of a single lipid A species on mass spectrometry and gave a single band on thin layer chromatography. The activity of purified lipid A species was examined using human and mouse cell lines that express recombinant human TLR4. Compared with unmodified lipid A, the modified lipid A species are 30-100-fold less active in the ability to induce NF-kappaB-dependent reporter activation. These results suggest that the lipid A modifications reduce TLR4-signaling as part of Salmonellae adaptation to host environments. | lld:pubmed |
| pubmed-article:15014080 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15014080 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15014080 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15014080 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15014080 | pubmed:month | May | lld:pubmed |
| pubmed-article:15014080 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15014080 | pubmed:author | pubmed-author:MillerSamuel... | lld:pubmed |
| pubmed-article:15014080 | pubmed:author | pubmed-author:KawasakiKiyos... | lld:pubmed |
| pubmed-article:15014080 | pubmed:author | pubmed-author:ErnstRobert... | lld:pubmed |
| pubmed-article:15014080 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15014080 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:15014080 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:15014080 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15014080 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15014080 | pubmed:pagination | 20044-8 | lld:pubmed |
| pubmed-article:15014080 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:15014080 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15014080 | pubmed:articleTitle | 3-O-deacylation of lipid A by PagL, a PhoP/PhoQ-regulated deacylase of Salmonella typhimurium, modulates signaling through Toll-like receptor 4. | lld:pubmed |
| pubmed-article:15014080 | pubmed:affiliation | Department of Microbiology, University of Washington, Seattle, WA 98195, USA. | lld:pubmed |
| pubmed-article:15014080 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15014080 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15014080 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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