toward α-2 gliadin. A 26 residue proteolytic resistance fragment has been found on γ-5 gliadin, positions 26–51, that has multiple transglutaminase and T-cell epitopes. This site has five overlapping T-cells sites of DQ2-"γ-II", -"γ-III", -"γ-IV", and "γ-glia 2". Computer analysis of 156 prolamins and glutelins revealed many more resistant fragments; one, a γ-gliadin, containing 4 epitopes was 68 amino acids in length. DQ2 and glutelins Triticeae glutelins presented by DQ2 is some coeliacs. In wheat, the low molecular weight glutenins often share structural similarity with the prolamins of the similar species of Triticeae. Two motifs, K1-like (46-60), pGH3-like (41-59) and GF1(33-51) have been identified. High molecular weight glutenin has also been identified as a potentially toxic protein Some of the HMW glutenins increase response with transglutaminase treatment, indicating the sites might be similar to alpha-gliadin and gamma gliadin T-cell sites. DQ2.2 restricted gliadin sites DQ2.2 can present a fewer number of lower affinity sites relative to DQ2.5. Some of these sites are found on γ-gliadin the gliadin most similar to prolamins of other Triticeae genera, a gliadin that appears to similar to ancestral. Antigen presenting cells bearing DQ2.2 can present alpha gliadin sites, for example alpha-II region of the "33mer" and therefore the "33mer" may have a role in DQ2.2 bearing individuals, but the binding capacity is substantially lower. HLA-DQ8 HLA-DQ8 confers susceptibility to coeliac disease but in a fashion somewhat similar to DQ2.5. Homozygotes of DQ8, DQ2.5/DQ8 and DQ8/DQ2.2 are higher than expected based on levels in the general population.(see: Understanding DQ haplotypes and DQ isoforms). HLA-DQ8 is generally not as involved in the most severe complications, and it does not recognize the "33mer" of α-2 gliadin to the same degree as DQ2.5. There are a smaller number of gliadin (prolamin) peptides presented by HLA-DQ8. A few studies have been done on the adaptive immune response for DQ8/DQ2- individuals. DQ8 appears to rely much more on adaptive immunity to the carboxyl half of alpha gliadins. In addition, it appear 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 coeliac disease. 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