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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
1990-11-21
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pubmed:abstractText |
The HLA-DR2 restriction of the T cell response to myelin basic protein (MBP) was studied using murine L cells transfected with DRalpha and either DR2a or DR2b beta-chain cDNA. DR2a and DR2b represent the two isotypic DRbeta chains expressed in DR2Dw2 haplotypes. Eleven MBP-specific cytolytic T cell lines derived from patients with multiple sclerosis were isolated. Two of these cell lines recognized MBP-pulsed DR2-expressing L cell transfectants and four of them could only recognize the L cells if the adhesion molecule ICAM-1 was expressed in addition to HLA-DR2. Five of the six lines were restricted by HLA-DR2a; one line recognized Ag in conjunction with DR2b, but only if ICAM-1 was coexpressed. The remaining five lines did not lyse MBP-pulsed L cells. The ability of the DR2b molecules on transfected cells to stimulate T cells was confirmed with DR2b-allospecific T cell clones. Although five MBP-specific lines were restricted by DR2a, they recognized different parts of the MBP molecule, as demonstrated by the presentation of shorter peptides. Thus, our results suggest that DR2a is a dominant restriction molecule in MBP-specific responses by DR2+ MS patients. The results also indicate that the reported heterogeneity in MBP epitopes recognized by DR2-restricted T cells, may not be due to the use of different restriction elements but rather to the binding of different MBP peptides to DR2a molecules.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Autoantigens,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DR2 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Adhesion Molecule-1,
http://linkedlifedata.com/resource/pubmed/chemical/Myelin Basic Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
145
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2880-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1698864-Animals,
pubmed-meshheading:1698864-Autoantigens,
pubmed-meshheading:1698864-Cell Adhesion Molecules,
pubmed-meshheading:1698864-Cell Line,
pubmed-meshheading:1698864-Cytotoxicity, Immunologic,
pubmed-meshheading:1698864-Epitopes,
pubmed-meshheading:1698864-HLA-DR2 Antigen,
pubmed-meshheading:1698864-Haplotypes,
pubmed-meshheading:1698864-Humans,
pubmed-meshheading:1698864-Intercellular Adhesion Molecule-1,
pubmed-meshheading:1698864-L Cells (Cell Line),
pubmed-meshheading:1698864-Lymphocyte Activation,
pubmed-meshheading:1698864-Mice,
pubmed-meshheading:1698864-Myelin Basic Proteins,
pubmed-meshheading:1698864-T-Lymphocytes, Cytotoxic,
pubmed-meshheading:1698864-Transfection
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pubmed:year |
1990
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pubmed:articleTitle |
HLA-DR2a is the dominant restriction molecule for the cytotoxic T cell response to myelin basic protein in DR2Dw2 individuals.
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pubmed:affiliation |
Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892.
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pubmed:publicationType |
Journal Article,
In Vitro
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