Source:http://linkedlifedata.com/resource/pubmed/id/10700238
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2000-3-22
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pubmed:abstractText |
Celiac disease (CD) is an increasingly diagnosed enteropathy (prevalence, 1:200-1:300) that is induced by dietary exposure to wheat gliadins (as well as related proteins in rye and barley) and is strongly associated with HLA-DQ2 (alpha1*0501, beta1*0201), which is present in over 90% of CD patients. Because a variety of gliadin peptides have been identified as epitopes for gliadin-specific T-cell clones and as bioactive sequences in feeding studies and in ex vivo CD intestinal biopsy challenge, it has been unclear whether a 'dominant' T-cell epitope is associated with CD. Here, we used fresh peripheral blood lymphocytes from individual subjects undergoing short-term antigen challenge and tissue transglutaminase-treated, overlapping synthetic peptides spanning A-gliadin to demonstrate a transient, disease-specific, DQ2-restricted, CD4 T-cell response to a single dominant epitope. Optimal gamma interferon release in an ELISPOT assay was elicited by a 17-amino-acid peptide corresponding to the partially deamidated peptide of A-gliadin amino acids 57-73 (Q65E). Consistent with earlier reports indicating that host tissue transglutaminase modification of gliadin enhances gliadin-specific CD T-cell responses, tissue transglutaminase specifically deamidated Q65 in the peptide of A-gliadin amino acids 56-75. Discovery of this dominant epitope may allow development of antigen-specific immunotherapy for CD.
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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/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Gliadin,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DQ Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DQ2 antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-10,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Transglutaminases
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1078-8956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
337-42
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10700238-Adult,
pubmed-meshheading:10700238-Age of Onset,
pubmed-meshheading:10700238-Amino Acid Sequence,
pubmed-meshheading:10700238-Celiac Disease,
pubmed-meshheading:10700238-Cells, Cultured,
pubmed-meshheading:10700238-Epitopes,
pubmed-meshheading:10700238-Female,
pubmed-meshheading:10700238-Gliadin,
pubmed-meshheading:10700238-Great Britain,
pubmed-meshheading:10700238-HLA-DQ Antigens,
pubmed-meshheading:10700238-Humans,
pubmed-meshheading:10700238-Interferon-gamma,
pubmed-meshheading:10700238-Interleukin-10,
pubmed-meshheading:10700238-Lymphocyte Activation,
pubmed-meshheading:10700238-Lymphocytes,
pubmed-meshheading:10700238-Male,
pubmed-meshheading:10700238-Middle Aged,
pubmed-meshheading:10700238-Molecular Sequence Data,
pubmed-meshheading:10700238-Peptide Fragments,
pubmed-meshheading:10700238-Prevalence,
pubmed-meshheading:10700238-T-Lymphocytes,
pubmed-meshheading:10700238-Transglutaminases
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pubmed:year |
2000
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pubmed:articleTitle |
In vivo antigen challenge in celiac disease identifies a single transglutaminase-modified peptide as the dominant A-gliadin T-cell epitope.
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pubmed:affiliation |
Institute of Molecular Medicine, Nuffield Department of Medicine, John Radcliffe Hospital, University of Oxford, Oxford OX3 9DU, UK. bob.anderson@ndm.ox.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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