Gluten Immunochemistry - Antibody Recognition

Antibody Recognition

Antibody recognition of gluten is complex. Direct binding to gluten such as anti-gliadin antibodies has an ambiguous pathogenesis in coeliac disease. The crosslinking of gliadin with tissue transglutaminase leads to the production of anti-transglutaminase antibodies, but this is mediated through T-cell recognition of gliadin. The allergic recognition of gliadin by mast cells, eosinophiles in the presence of IgE has notable direct consequences, such as exercise-induced anaphylaxis.

Anti-gliadin antibodies, like those detected in celiac disease bind to the α-2 gliadin(57-73). This site is within the T-cell reactive "33mer" presented by DQ2.5. There has been some suggestion wheat plays a role in juvenile diabetes as antibodies to the non-glutinous seed storage glb-1 (a globulin) are implicated in crossreactive autoantigenic antibodies that destroy islet cells in the pancreas. Anti-gliadin antibodies have been found to synapsin I Omega-gliadin and the HMW Glutenin subunit antibodies have been found most commonly in individuals with exercise-induced anaphylaxis and Baker's allergy, and represent a potent class of gluten allergens. Non-glutinous proteins in wheat are also allergens, these include: LTP (albumin/globulin), thioredoxin-hB, and wheat flour peroxidase. A particular 5 residue peptide, Gln-Gln-Gln-Pro-Pro motif, has been found to be a major wheat allergen.

Read more about this topic:  Gluten Immunochemistry

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