ИСТИНА

The term gluten intolerance may refer to three types of human disorders: autoimmune celiac disease (СВ), allergy to wheat and non-celiac gluten sensitivity. Th e global prevalence of CD is estimated at approximately 1%. Digested in gastrointestinal tract wheat gluten-derived peptides or peptides derived from related proteins of barley, rye or oat (horedeins, secalins and avenins, respectively) are the inducers of these diseases in predisposed subjects. Currently, the only treatment available is a permanent strict gluten-free diet. Wheat gluten and related proteins from other grains function as major seed storage proteins. To support the growing plantlets with amino acids, still mostly uncharacterized proteolytic enzymes are involved in gluten-related proteins digestion. Potentially such enzymes can be employed for gluten detoxifi cation in medical use and biotechnological applications. A number of mRNAs encoding proteolytic enzymes are detected in growing wheat seedlings. One of these mRNAs encodes papain-like cysteine protease Triticain-α. In the present work, we cloned Triticain-α gene, and revealed optimal domain organization for the proenzyme resulting in the maturation of an active protease exhibiting pronounced glutenase activity. Biochemical and massspectrometry analysis of the products of Triticain-α-catalyzed gluten hydrolysis revealed multiple cleavage sites withinthe sequences of gliadin toxic peptides, in particular, in the major toxic 33-mer α-gliadin-derived peptide initiating infl ammatory responses to gluten in celiac disease patients. Triticain-α was found to be relatively stable in the conditions simulating stomach environment. We conclude that Triticain-α can be exploited as a basic compound for development of (i) pharmaceuticals for celiac disease treatment, and (ii) biotechnological applications in gluten-free food manufacturing.