Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2008-8-1
pubmed:abstractText
Recognition of LPS depends on the interaction of at least three molecules forming the LPS-receptor complex. The most important ones, CD14, MD2 and Toll-like receptor (TLR) 4 share a high degree of homology between species. In the present study, we investigated the importance of species-specific restriction on the recognition of LPS using stably transfected HEK293 cell lines expressing either human or bovine LPS-receptor complex components. Species-specific MD2 appeared to confer LPS recognition, whereas species-specific CD14 only appeared to play a minor role. In addition to the recognition of LPS, there is evidence that the fusion (F) protein of respiratory syncytial virus (RSV), which is the most common viral respiratory pathogen during infancy world-wide, interacts with TLR4, and plays an important role in the initiation of the innate immune response. Our findings suggest that human and bovine RSV may activate human and bovine TLR4 receptors, respectively, in the presence of both MD2 and CD14. However, no clear role for the RSV F protein of either human or bovine RSV alone in stimulating TLR4-dependent NF-kappaB activation was observed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1753-4259
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
223-31
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed-meshheading:18669608-Animals, pubmed-meshheading:18669608-Antigens, CD14, pubmed-meshheading:18669608-Cattle, pubmed-meshheading:18669608-Cell Line, pubmed-meshheading:18669608-Enzyme Activation, pubmed-meshheading:18669608-Humans, pubmed-meshheading:18669608-Immunity, Innate, pubmed-meshheading:18669608-Interleukin-8, pubmed-meshheading:18669608-Lipopolysaccharides, pubmed-meshheading:18669608-Lymphocyte Antigen 96, pubmed-meshheading:18669608-Mice, pubmed-meshheading:18669608-Multiprotein Complexes, pubmed-meshheading:18669608-Protein-Serine-Threonine Kinases, pubmed-meshheading:18669608-Respiratory Syncytial Viruses, pubmed-meshheading:18669608-Signal Transduction, pubmed-meshheading:18669608-Species Specificity, pubmed-meshheading:18669608-Toll-Like Receptor 4, pubmed-meshheading:18669608-Transfection, pubmed-meshheading:18669608-Transgenes
pubmed:year
2008
pubmed:articleTitle
Host species-specific usage of the TLR4-LPS receptor complex.
pubmed:affiliation
Royal Veterinary College, Hawkshead Campus, Hatfield, UK.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't