Gliadin and related gluten proteins (Gluten)

Gliadin and related gluten proteins, including glutenins, hordeins, and secalins, are the primary storage proteins found in wheat, barley, and rye (Scherf et al., 2016). These proteins are uniquely high in proline and glutamine residues, a structural feature that renders them highly resistant to complete proteolysis by human digestive enzymes (Lebwohl et al., 2018). In individuals with Celiac disease, the resulting undigested peptides—most notably the 33-mer fragment—translocate across the intestinal barrier and are deamidated by tissue transglutaminase 2 (TG2), enhancing their recognition by HLA-DQ2/DQ8-positive immune cells (Sollid et al., 2012). This recognition triggers an inflammatory cascade that leads to intestinal villous atrophy and systemic autoimmunity. Beyond Celiac disease, these proteins are the causative agents in wheat allergy and non-celiac gluten sensitivity (Sapone et al., 2012). Therapeutic strategies targeting these proteins focus on neutralizing their immunogenicity, primarily through oral glutenases like latiglutenase that degrade the peptides in the stomach, or through sequestering polymers and immune-tolerance-inducing nanoparticles (Syage et al., 2017; Kelly et al., 2021).

Other names

ProlaminsGlutenWheat storage proteinsHordeinsSecalinsAveninsGlutenins

Enzymatic degradation of immunogenic peptides, sequestration to prevent intestinal absorption, and induction of immune tolerance.