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Industrial processes enabling the diversification of the food protein functionalities can modify their allergenicity. In animal models, enzymatic hydrolysis of gliadins, the major allergens of wheat gluten, reduces their allergenic potential or leaves it unchanged, whereas deamidation of gliadins was associated with severe allergic reactions.

We do not have enough hard science to link the biochemical characteristics of food proteins with their capacity to direct an immune response towards allergy or tolerance.

Compounding the issue, there is still no validated in vitro test that could serve to assess the effect of food protein modifications on allergenicity and ultimately to assess the risk of new engineered ingredients triggering new allergies.

Working in collaboration with Dutch researchers on the COST Acton ImpARAS (Improved Allergenicity Risk Assessment Strategy), we brought in vitro dendritic cells into contact with native, enzymatically-hydrolyzed or deaminated gliadins.

Native gliadins have an immunostimulatory effect: they induce dendritic cell expression of several compounds involved in initiating immune responses- including compounds that help activate T-cells or help dendritic cells migrate towards the organs where the allergic response will express.

Enzymatic hydrolysis and, to a lesser extent, deamidation lead to a decrease in the molecular weight of gliadins. In both cases, there is a loss of native gliadin epitopes, i.e. of antigenic sites in wheat allergy, but deamidation also generates new epitopes.

Both enzymatic hydrolysis and deamidation are therefore found to heavily modify certain key properties of gliadins and gliadin-dendritic cell interactions.