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  4. Τμήμα Ιατρικής
  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/18058
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dc.contributor.authorMoustakas, A. K.en
dc.contributor.authorvan de Wal, Y.en
dc.contributor.authorRoutsias, J.en
dc.contributor.authorKooy, Y. M.en
dc.contributor.authorvan Veelen, P.en
dc.contributor.authorDrijfhout, J. W.en
dc.contributor.authorKoning, F.en
dc.contributor.authorPapadopoulos, G. K.en
dc.date.accessioned2015-11-24T18:50:22Z-
dc.date.available2015-11-24T18:50:22Z-
dc.identifier.issn0953-8178-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/18058-
dc.rightsDefault Licence-
dc.subjectAllelesen
dc.subjectAmino Acid Sequenceen
dc.subjectAmino Acid Substitutionen
dc.subjectAntigen Presentationen
dc.subjectAutoantigens/immunologyen
dc.subjectAutoimmune Diseases/genetics/*immunologyen
dc.subjectBinding Sitesen
dc.subjectCeliac Disease/genetics/*immunologyen
dc.subjectEpitopes/chemistry/*immunologyen
dc.subject*Genes, MHC Class IIen
dc.subjectGenetic Predisposition to Diseaseen
dc.subjectGliadin/chemistry/*immunologyen
dc.subjectGlutens/*analogs & derivatives/chemistry/*immunologyen
dc.subjectHLA-DQ Antigens/chemistry/*genetics/immunologyen
dc.subjectIntestinal Mucosa/immunologyen
dc.subjectLymphocyte Activationen
dc.subjectModels, Molecularen
dc.subjectMolecular Mimicryen
dc.subjectMolecular Sequence Dataen
dc.subjectPeptide Fragments/chemistry/immunologyen
dc.subjectPolymorphism, Geneticen
dc.subjectProtein Conformationen
dc.subjectSequence Alignmenten
dc.subjectSequence Homology, Amino Aciden
dc.subjectStructure-Activity Relationshipen
dc.titleStructure of celiac disease-associated HLA-DQ8 and non-associated HLA-DQ9 alleles in complex with two disease-specific epitopesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/10917890-
heal.identifier.secondaryhttp://intimm.oxfordjournals.org/content/12/8/1157.full.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2000-
heal.abstractThe association of celiac disease (CD) with HLA-DQ2 and HLA-DQ8 is indicative of preferential mucosal T cell recognition of gluten fragments bound to either DQ allele. We have recently identified two gluten-derived, HLA-DQ8-restricted T cell stimulatory peptides, one each from gliadin and glutenin, recognized by specific T cell clones derived from the small intestine of CD patients. We have now performed molecular modeling and examined the fine specificity of these peptides in complex with HLA-DQ8. There is only one binding register for both peptides, with glutamine residues at the p1 and p9 anchor positions. Both T cell clones recognize substituted peptides at p1 and p9, but poorly so at p2-p8, especially the gliadin-specific clone. Contrasting patterns of recognition of p9Gln --> Glu peptide variants (both predicted as better DQ8 binders by modeling) were observed: enhancement of recognition for the gliadin peptide, yet complete absence thereof for the glutenin peptide. The double-substituted gliadin peptide variant p1/9Gln --> Glu, which can also arise by pepsin/acid/transglutaminase treatment, shows a considerable increase in sensitivity of recognition, consistent with better binding of this peptide to DQ8, as predicted by energy minimization. Surprisingly, the two native peptides are also recognized by their respective T cell clones in the context of the related molecule HLA-DQ9 (beta57Asp(+)). The p1/9Gln --> Glu gliadin peptide variant is likewise recognized, albeit with a 10-fold lower sensitivity, the first reported p9Glu binding in a beta57Asp(+) MHC II allele. Our results have important implications for the pathogenesis of autoimmune disease and the possible manipulation of aberrant responses thereof.en
heal.journalNameInt Immunolen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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