Sela B
Institute of Pathological Chemistry, Haim Sheba Medical Center, Tel Hashomer, Israel.
Harefuah. 2003 Jul;142(7):554-7, 564.
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.
最近的研究已指出麦醇溶蛋白上的一段相关序列，其可能作为乳糜泻中的免疫显性表位。几家顶尖实验室的独立报告确定了一个跨越第57至89位残基的33个氨基酸片段，该片段脯氨酸和谷氨酰胺含量过高，为假定表位。第65位的谷氨酰胺残基是转谷氨酰胺酶脱酰胺作用的位点，促进其被DQ2-HLA识别。此外，另一种麸质蛋白，即麦谷蛋白，可能与乳糜泻的发病机制有关。
