Wheat gluten protein (Gluten)

Wheat gluten proteins, primarily composed of gliadins and glutenins, are the major storage proteins found in wheat. These proteins are characterized by a high content of proline and glutamine residues, which renders them highly resistant to complete digestion by human gastrointestinal proteases (https://pubmed.ncbi.nlm.nih.gov/19515230/). In individuals with Celiac disease, the resulting long peptide fragments are deamidated by tissue transglutaminase and presented by HLA-DQ2 or HLA-DQ8 molecules, triggering an inflammatory T-cell response that leads to intestinal villous atrophy (https://www.niddk.nih.gov/health-information/digestive-diseases/celiac-disease). From a therapeutic perspective, wheat gluten proteins serve as exogenous targets for oral enzyme replacement therapies, such as latiglutenase, which aim to degrade these immunogenic peptides into smaller, non-toxic fragments before they reach the small intestine (https://clinicaltrials.gov/ct2/show/NCT01917630). Other strategies involve using polymers to sequester gluten or tight-junction regulators to prevent its translocation across the epithelial barrier. While not an endogenous human receptor or enzyme, gluten is the primary driver of several autoimmune and allergic pathologies, making its neutralization or degradation a significant focus in gastroenterological drug development.

Other names

GlutenGliadinGluteninTriticum aestivum storage proteinsProlamins

Enzymatic degradation of immunogenic peptides (proteolysis), reduction of intestinal permeability to prevent protein translocation, and sequestration of antigenic fragments.