Gluten antigens (Gluten)

Gluten antigens refer to a complex group of storage proteins found in wheat, barley, and rye, primarily categorized into alcohol-soluble gliadins and alcohol-insoluble glutenins [1.1.3, 1.1.5]. These proteins are characterized by a high content of proline and glutamine residues, which renders them resistant to complete proteolysis by human digestive enzymes, resulting in the persistence of large, immunogenic peptide fragments in the small intestine [1.1.5, 1.2.2]. In individuals with Celiac disease, these peptides are deamidated by the enzyme tissue transglutaminase 2 (TG2), significantly increasing their binding affinity for HLA-DQ2 or HLA-DQ8 molecules on antigen-presenting cells [1.1.3, 1.2.4]. This presentation triggers a T-cell mediated inflammatory response that leads to intestinal villous atrophy, mucosal damage, and systemic symptoms [1.1.3, 1.4.4]. Therapeutic interventions targeting gluten antigens aim to neutralize their toxicity through the use of exogenous oral proteases (glutenases) that degrade the peptides, sequestering agents that prevent their absorption, or nanoparticle-based platforms designed to reprogram the immune system toward tolerance [1.2.1, 1.4.1].

Other names

GliadinGluteninProlaminsWheat gluten proteinsTriticeae glutens

Enzymatic degradation (proteolysis) of immunogenic peptides, induction of antigen-specific immune tolerance, and sequestration within the gastrointestinal lumen.