Source:http://linkedlifedata.com/resource/pubmed/id/10359111
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1999-6-30
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class I,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class II,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell...,
http://linkedlifedata.com/resource/pubmed/chemical/Superantigens,
http://linkedlifedata.com/resource/pubmed/chemical/stinging nettle lectin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-2980
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
29
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1571-80
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10359111-Animals,
pubmed-meshheading:10359111-Antigen Presentation,
pubmed-meshheading:10359111-Cell Division,
pubmed-meshheading:10359111-Female,
pubmed-meshheading:10359111-Histocompatibility Antigens Class I,
pubmed-meshheading:10359111-Histocompatibility Antigens Class II,
pubmed-meshheading:10359111-Lectins,
pubmed-meshheading:10359111-Mice,
pubmed-meshheading:10359111-Mice, Inbred C57BL,
pubmed-meshheading:10359111-Plant Lectins,
pubmed-meshheading:10359111-Receptors, Antigen, T-Cell, alpha-beta,
pubmed-meshheading:10359111-Signal Transduction,
pubmed-meshheading:10359111-Solubility,
pubmed-meshheading:10359111-Superantigens,
pubmed-meshheading:10359111-T-Lymphocytes
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pubmed:year |
1999
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pubmed:articleTitle |
Major histocompatibility class I molecules present Urtica dioica agglutinin, a superantigen of vegetal origin, to T lymphocytes.
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pubmed:affiliation |
Unité d'Immunophysiologie Moléculaire, Institut Pasteur, Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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