[The identification of the immunodominant gliadin epitope].
Recent efforts have piri-pointed a relevant sequence on gliadin, that may act as the immunodominant epitope in celiac disease. Independent reports from several leading laboratories identify a 33 amino acid segment spanning through residues 57-89, and excessively rich in proline and glutamine, as the putative epitope. A glutamine residue in position 65 is the site of deamidation by transglutaminase, promoting its recognition by DQ2-HLA. In addition, another gluten protein, glutenin, may be relevant to the pathogenesis in celiac disease.
Sela
B
B
Institute of Pathological Chemistry, Haim Sheba Medical Center, Tel Hashomer, Israel.
D000595:Amino Acid Sequence; D002446:Celiac Disease / Q000276:immunology*; D000939:Epitopes / Q000737:chemistry; D005903:Gliadin / Q000276:immunology*; D005973:Glutamine; D006683:HLA-DQ Antigens / Q000276:immunology; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000276:immunology; D011392:Proline
D000939:Epitopes; D006683:HLA-DQ Antigens; C053186:HLA-DQ2 antigen; D010446:Peptide Fragments; D005973:Glutamine; D005903:Gliadin; D011392:Proline