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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1991-5-29
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pubmed:abstractText |
The fine specificity of two human T cell clones responding to autologous HLA-DR1 expressing antigen-presenting cells (APC) in the absence of nominal antigen has been investigated using Epstein-Barr virus-transformed B cells (BCL) of known DR beta 1 domain sequence. It was found that responsiveness was markedly affected by changes in a limited number of residues in this domain. Substitution of the DR1 beta sequence at one residue, position 74, even conservatively, was found to be particularly significant. Located on the beta 1 domain alpha-helix, this residue is predicted to point into the antigen-binding groove and is therefore unlikely to make contact with the T cell receptor. This finding suggests that these T cells are specific for a bound endogenous peptide within the autologous major histocompatibility (MHC) binding groove. The autospecific T cell clones also responded to murine L cell transfectants expressing DR alpha DR1 beta as well as to transfectants expressing the mouse/human hybrid MHC molecule I-E alpha DR1 beta but not to the reciprocal combination DR alpha I-E beta, thus confirming the importance of the beta 1 domain to T cell recognition. In contrast to the autocytotoxicity observed with BCL, cytolysis of the murine L cells expressing the HLA-DR1 molecule was slight and only found at high effector-target ratios. In addition, although fixation enhanced the recognition of BCL, capacity of the murine L cells bearing the HLA-DR1 molecule to stimulate T cell clone proliferation was markedly reduced by aldehyde fixation. When taken together, these results suggest that the endogenous peptides recognized by these autoreactive T cells are of human origin.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0953-8178
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
624-30
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:2489049-Amino Acid Sequence,
pubmed-meshheading:2489049-Animals,
pubmed-meshheading:2489049-Antigen-Presenting Cells,
pubmed-meshheading:2489049-Antigens, CD4,
pubmed-meshheading:2489049-Autoantigens,
pubmed-meshheading:2489049-Clone Cells,
pubmed-meshheading:2489049-Cytotoxicity, Immunologic,
pubmed-meshheading:2489049-HLA-DR1 Antigen,
pubmed-meshheading:2489049-Humans,
pubmed-meshheading:2489049-L Cells (Cell Line),
pubmed-meshheading:2489049-Lymphocyte Activation,
pubmed-meshheading:2489049-Molecular Sequence Data,
pubmed-meshheading:2489049-Peptides,
pubmed-meshheading:2489049-T-Lymphocytes
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pubmed:year |
1989
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pubmed:articleTitle |
Functional evidence for the recognition of endogenous peptides by autoreactive T cell clones.
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pubmed:affiliation |
MRC Tuberculosis and Related Infections Unit, Hammersmith Hospital, London, UK.
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pubmed:publicationType |
Journal Article
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