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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1991-10-11
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pubmed:abstractText |
It has been shown that two different sites (an agretope and an epitope) on a peptide antigen function independently in T cell responses to the antigen. By virtue of these sites, antigens, MHC molecules, and TCRs constitute trimolecule complexes which eventually result in T cell activation. In our previous reports, we have defined that residues 46 and 54 on synthetic peptide composed of residues 43-58 of pigeon cytochrome c (p43-58, AEGFSYTDANKNKGIT) and its analogs function as an agretope and residue 50 as an epitope in both I-Ab and I-Ak-carrying mice. In the present study, to extend our method to the other MHC class II molecules (I-E), we used two peptide antigens, 46D50V54R and 50V54R, which had been prepared by substitution of amino acids at positions, 46, 50 and 54 or 50 and 54 of p43-58 D, V, R or V, R, respectively, and compared the immunogenicity with those of other peptide analogs. The 46D50V54R was shown to be non-immunogenic in I-Ab-carrying mice and the 50V54R was non-immunogenic in I-Ak-carrying mice. In contrast, the 46D50V54R or 50V54R could induce I-E-restricted proliferative responses of T lymphocytes in I-Eb/k- or I-Ek/k-carrying mice, respectively. Furthermore, residues 46 and 54 were shown to function as agretopes and residue 50 as an epitope in the I-E-restricted responses as they did in the I-A-restricted responses, even though some differences were seen between peptide-I-E interaction and peptide-I-A interaction. These agretopes and epitope functioned independently.
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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/Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class II,
http://linkedlifedata.com/resource/pubmed/chemical/I-E-antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0953-8178
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
503-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1716143-Amino Acid Sequence,
pubmed-meshheading:1716143-Animals,
pubmed-meshheading:1716143-Antigens,
pubmed-meshheading:1716143-Binding Sites,
pubmed-meshheading:1716143-Cytochrome c Group,
pubmed-meshheading:1716143-Epitopes,
pubmed-meshheading:1716143-Histocompatibility Antigens Class II,
pubmed-meshheading:1716143-Lymphocyte Activation,
pubmed-meshheading:1716143-Mice,
pubmed-meshheading:1716143-Molecular Sequence Data,
pubmed-meshheading:1716143-Peptides,
pubmed-meshheading:1716143-T-Lymphocytes
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pubmed:year |
1991
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pubmed:articleTitle |
Analysis of functional sites on a peptide antigen, p43-58, in I-A or I-E-restricted T cell responses.
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pubmed:affiliation |
Institute of Immunological Science, Hokkaido University, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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