| pubmed-article:10359111 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10359111 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
| pubmed-article:10359111 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
| pubmed-article:10359111 | lifeskim:mentions | umls-concept:C0206527 | lld:lifeskim |
| pubmed-article:10359111 | lifeskim:mentions | umls-concept:C0019627 | lld:lifeskim |
| pubmed-article:10359111 | lifeskim:mentions | umls-concept:C0439659 | lld:lifeskim |
| pubmed-article:10359111 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
| pubmed-article:10359111 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:10359111 | lifeskim:mentions | umls-concept:C0075260 | lld:lifeskim |
| pubmed-article:10359111 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:10359111 | pubmed:dateCreated | 1999-6-30 | lld:pubmed |
| pubmed-article:10359111 | pubmed:abstractText | The Urtica dioica agglutinin (UDA) shares with the superantigens the property of activating T cell subsets bearing particular Vbeta segments of the TCR. However, UDA is a lectin capable of binding to many glycoproteins on cell membranes. The implication of MHC versus other glycoproteins in UDA presentation was presently studied. Using mutant mice lacking MHC class I (MHC-I), MHC class II (MHC-II) or both MHC antigens, we provided evidence that MHC-I and MHC-II molecules serve as UDA receptors. Presentation by either one of these molecules ensured similar T cell responses and co-stimulatory signals were mandatory for optimal T cell activation and proliferation both in MHC-I and MHC-II contexts. Remarkably, in the absence of MHC molecules, UDA could not be efficiently presented to T cells by other glycosylated proteins. Surface plasmon resonance studies were used to confirm the binding of UDA to MHC-I molecules using a fusion protein consisting of MHC-I domains and beta2-microglobulin. The results indicated that the interaction between UDA and MHC-I molecules implicated lectin-binding site(s) of UDA. Taken together, our data demonstrate that, in addition to MHC-II antigens, MHC-I molecules serve as an alternative ligand for UDA. | lld:pubmed |
| pubmed-article:10359111 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10359111 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10359111 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10359111 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10359111 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10359111 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10359111 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10359111 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10359111 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10359111 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10359111 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10359111 | pubmed:month | May | lld:pubmed |
| pubmed-article:10359111 | pubmed:issn | 0014-2980 | lld:pubmed |
| pubmed-article:10359111 | pubmed:author | pubmed-author:Truffa-BachiP... | lld:pubmed |
| pubmed-article:10359111 | pubmed:author | pubmed-author:PeumansW JWJ | lld:pubmed |
| pubmed-article:10359111 | pubmed:author | pubmed-author:BuckleMM | lld:pubmed |
| pubmed-article:10359111 | pubmed:author | pubmed-author:AbastadoJ PJP | lld:pubmed |
| pubmed-article:10359111 | pubmed:author | pubmed-author:RoviraPP | lld:pubmed |
| pubmed-article:10359111 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10359111 | pubmed:volume | 29 | lld:pubmed |
| pubmed-article:10359111 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10359111 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10359111 | pubmed:pagination | 1571-80 | lld:pubmed |
| pubmed-article:10359111 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10359111 | pubmed:meshHeading | pubmed-meshheading:10359111... | lld:pubmed |
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| pubmed-article:10359111 | pubmed:meshHeading | pubmed-meshheading:10359111... | lld:pubmed |
| pubmed-article:10359111 | pubmed:meshHeading | pubmed-meshheading:10359111... | lld:pubmed |
| pubmed-article:10359111 | pubmed:meshHeading | pubmed-meshheading:10359111... | lld:pubmed |
| pubmed-article:10359111 | pubmed:meshHeading | pubmed-meshheading:10359111... | lld:pubmed |
| pubmed-article:10359111 | pubmed:meshHeading | pubmed-meshheading:10359111... | lld:pubmed |
| pubmed-article:10359111 | pubmed:meshHeading | pubmed-meshheading:10359111... | lld:pubmed |
| pubmed-article:10359111 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10359111 | pubmed:articleTitle | Major histocompatibility class I molecules present Urtica dioica agglutinin, a superantigen of vegetal origin, to T lymphocytes. | lld:pubmed |
| pubmed-article:10359111 | pubmed:affiliation | Unité d'Immunophysiologie Moléculaire, Institut Pasteur, Paris, France. | lld:pubmed |
| pubmed-article:10359111 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10359111 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
