Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2004-12-13
pubmed:abstractText
The Salmonella typhimurium virulence gene products, PhoP/PhoQ sense host micro-environments to regulate the expression of a lipid A 3-O-deacylase, PagL, and a lipid A palmitoyltransferase, PagP. Therefore, deacylation and/or palmitoylation of lipid A could occur in Salmonellae adapted to host environments. The acylation state of lipid A can alter host recognition and signaling by Toll-like receptor (TLR) 4, and may play an important role in host defenses against Salmonellae infection. Deacylated lipid A, deacylated and palmitoylated lipid A, palmitoylated lipid A, and unmodified lipid A species were purified, and the activity was examined using cell lines expressing recombinant human or mouse TLR4. Compared with unmodified lipid A, the modified lipid A species are 10-100-fold less active. These results suggest that PagL and PagP modify lipid A to reduce TLR4-signaling as part of Salmonellae adaptation to the host environment.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carboxylic Ester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Lipid A, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/PagL protein, Salmonella typhimurium, http://linkedlifedata.com/resource/pubmed/chemical/PagP protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface, http://linkedlifedata.com/resource/pubmed/chemical/TLR4 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptor 4, http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptors
pubmed:status
MEDLINE
pubmed:issn
0968-0519
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
439-44
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:15588428-Acyltransferases, pubmed-meshheading:15588428-Animals, pubmed-meshheading:15588428-Bacterial Outer Membrane Proteins, pubmed-meshheading:15588428-Bacterial Proteins, pubmed-meshheading:15588428-Carboxylic Ester Hydrolases, pubmed-meshheading:15588428-Cell Line, pubmed-meshheading:15588428-Escherichia coli Proteins, pubmed-meshheading:15588428-Gene Expression Regulation, Enzymologic, pubmed-meshheading:15588428-Humans, pubmed-meshheading:15588428-Lipid A, pubmed-meshheading:15588428-Membrane Glycoproteins, pubmed-meshheading:15588428-Mice, pubmed-meshheading:15588428-Molecular Structure, pubmed-meshheading:15588428-Receptors, Cell Surface, pubmed-meshheading:15588428-Salmonella typhimurium, pubmed-meshheading:15588428-Signal Transduction, pubmed-meshheading:15588428-Spectrometry, Mass, Matrix-Assisted Laser..., pubmed-meshheading:15588428-Toll-Like Receptor 4, pubmed-meshheading:15588428-Toll-Like Receptors
pubmed:year
2004
pubmed:articleTitle
Deacylation and palmitoylation of lipid A by Salmonellae outer membrane enzymes modulate host signaling through Toll-like receptor 4.
pubmed:affiliation
Department of Microbiology, University of Washington, Seattle, Washington 98195, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.