Omega-gliadin and gamma-gliadin

Omega-gliadin and gamma-gliadin are alcohol-soluble prolamin proteins found in wheat that serve as essential nutrient storage for the plant embryo (UniProt P02865, P08453). In humans, these proteins are notoriously difficult to digest due to their high proline and glutamine content, which resists standard gastrointestinal proteolysis (Scherf et al., 2016). The resulting undigested peptides can cross the intestinal epithelial barrier, where they are deamidated by tissue transglutaminase 2, significantly increasing their immunogenicity in individuals carrying HLA-DQ2 or HLA-DQ8 alleles. This process triggers the inflammatory T-cell response characteristic of Celiac Disease and is also linked to wheat-dependent exercise-induced anaphylaxis, particularly involving the omega-5 gliadin fraction (Morita et al., 2003). Therapeutic strategies targeting these proteins include the development of oral proteases, such as Latiglutenase and TAK-062, designed to break down immunogenic epitopes within the stomach (Lahdeaho et al., 2014). Additionally, sequestering agents like BL-7010 are being explored to bind these proteins and prevent their interaction with the immune system. Peptide-based vaccines like Nexvax2 have also aimed to induce immune tolerance by exposing the immune system to specific gliadin epitopes (Tye-Din et al., 2010). These interventions represent a shift toward non-dietary management of gluten-related disorders by directly neutralizing the pathogenic trigger.

Other names

Omega-gliadinGamma-gliadinProlaminWheat gluten proteinGluten

Proteolytic degradation of immunogenic peptides, sequestration of proteins in the gut lumen, and induction of immune tolerance through peptide-based immunotherapy.