Gluten immunochemistry to react with gamma gliadin to a degree comparable to DQ2.5. T-cell responses to the high molecular weight glutenin may be more important with DQ8 mediated than DQ2.5 mediated celiac disease. 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
Anti-gliadin antibodies in food products. Some of these antibodies can recognize only wheat prolamins or very closely related grass seeds; others can detect antigens over broad taxa. The G12 antibody is the newest example which detects the most immunotoxic fragment, a 33-mer peptide from �-2 gliadin; available from Romer Laboratories and the Spanish company Biomedal. It recognizes the toxic fraction of wheat, barley, rye and also of oat. The R5 sandwich assay is another such assay. This assay can recognize wheat, barley and rye, which makes it ideal for evaluating the presence of contaminants in gluten-free foods that do not contain oat.