Transamidated gliadin stimulates intestinal IL-10 in vitro in untreated CD patients

A major hallmark of celiac disease (CD) is inappropriate intestinal T cell activation in DQ2 and DQ8 patients triggered by peptides from wheat gluten and related prolamins from barley and rye. Moreover, tTGase plays a crucial role in CD immune-mediated pathogenesis (1-2). A strategy for preventing tTGase activity on gliadins could be instrumental in blocking the pathogenic mechanisms that occur in CD. Interestingly, mTGase exhibit the same site specificity as tTGase but lacks deamidase activity. We have shown that transamidation of gliadin following the treatment of wheat flour with mTGase caused a dramatic down-regulation in IFN-g production in vitro in the intestinal T cells of CD patients (3). Herein, the effects of transamidated gliadin (spf) on the ongoing inflammatory response were tested in cultured intestinal specimens derived from untreated CD patients.