TITLE

IgA antibodies of coeliac disease patients recongnise a dominant T cell epitope of A-gliadin

AUTHOR(S)
Bateman, E. A. L.; Ferry, B. L.; Hall, A.; Misbah, S. A.; Anderson, R.; Kelleher, P.
PUB. DATE
September 2004
SOURCE
Gut;Sep2004, Vol. 53 Issue 9, p1274
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Background: In coeliac disease (CD) patients, the dominant DQ2-A-I-gliadin peptide recognized by CD4 T cells is contained within peptide sequence 57-73 (p57-73) of A-gliadin. This peptide sequence is also located within a 33-mer protease resistant gliadin fragment and therefore is likely to play an important role in the pathogenesis of CD. Aims: Our aim was to determine whether a B cell epitope was present within the immunodominant T cell epitope of A-gliadin and, if so, to elucidate its sequence and determine the importance of deamidation and/or modification of the amino acid at position 65 for IgA binding. Patients and Methods: A cohort of CD patients, disease controls, and healthy individuals were examined. Serum IgA antibodies to the native and modified p57-73 fragment of A-gliadin were analyzed using enzyme linked immunosorbent assays. Peptide scanning experiments were further used to elucidate the B cell epitope. Results and Conclusion: IgA antibodies to p57-73 were found in 29/72 (40.2%) endomysial antibody positive patients, all of whom had CD. The peptide antibody appeared to be present when patients were on a diet containing gluten and declined on a gluten free diet. The p57-73 antibody was very specific for CD (98%) and had a sensitivity of 56%. The amino acid at position 65 was not important for IgA binding but was crucial for T cell recognition of p57-73. Pentapeptide PXPQP emerges as a potentially strong candidate for the IgA binding motif in this region of A-gliadin. This study shows that a significant proportion of newly diagnosed CD patients have an antibody response to the immunodominant T cell epitope.
ACCESSION #
14434508

 

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