Impacts of Sourdough Technology on the Availability of Celiac Peptides from Wheat α- and γ-Gliadins: In Silico Approach

Abstract

Celiac peptide-generating α- and γ-gliadins consist of a disordered N-terminal domain extended by an α-helical-folded C-terminal domain. Celiac peptides, primarily located along the disordered part of α- and γ-gliadin molecules, are nicely exposed and directly accessible to proteolytic enzymes occurring in the gastric (pepsin) and intestinal (trypsin, chymotrypsin) fluids. More than half of the potential celiac peptides identified so far in gliadins exhibit cleavage sites for pepsin. However, celiac peptides proteolytically truncated by one or two amino acid residues could apparently retain some activity toward HLA-DQ2 and HLA-DQ8 receptors in docking experiments. Together with the uncleaved peptides, these still active partially degraded CD peptides account for the incapacity of the digestion process to inactivate CD peptides from gluten proteins. In contrast, sourdough fermentation processes involve other proteolytic enzymes susceptible to the deep degradation of celiac peptides. In particular, sourdough supplemented by fungal prolyl endoproteases enhances the degrading capacities of the sourdough fermentation process toward celiac peptides. Nevertheless, since tiny amounts of celiac peptides sufficient to trigger deleterious effects on CD people can persist in sourdough-treated bread and food products, it is advisable to avoid consumption of sourdough-treated food products for people suffering from celiac disease. As an alternative, applying the supplemented sourdough process to genetically modified low gluten or celiac-safe wheat lines should result in food products that are safer for susceptible and CD people.

A comprehensive review on mango allergy: Clinical relevance, causative allergens, cross‐reactivity, influence of processing techniques, and management strategies

“…Therefore, consuming fruit or vegetable allergens does not typically induce any reaction in sensitized individuals. Sensitization to pan‐allergens must be taken into account throughout their research, despite the fact that the clinical relevance is still debatable in this situation (Barre et al., 2023; Hauser et al., 2010).…”

“…The cross‐reactivities between allergens in fruits and similar proteins found in other vegetables, seeds, and pollen sources contribute to various food‐pollen syndromes (Figure 6). These syndromes primarily involve common allergens, such as profilins, Bet v 1 proteins, and seed storage proteins (Barre et al., 2023). Although these syndromes usually manifest as mild OAS, they can occasionally result in more severe systemic reactions.…”

“…Despite the fact that fruit allergies are frequently not severe, they are relatively more prevalent compared to other types of allergies, affecting approximately 4.3% of the population (Vanga et al., 2018). This high prevalence can be attributed to the fact that many major allergens found in fruits share a similar structure with vegetables, birch and other pollens (Barre et al., 2023). As previously mentioned, fruit allergies are prevalent in both children and adults, often occurring in individuals with pollen sensitivities.…”

“…Class I chitinases have emerged as the primary panallergens in fruits connected to the latex‐fruit syndrome, including avocado, banana, and chestnut. Nevertheless, the presence of these enzymes in other plant foods does not seem to be associated with this syndrome, mainly due to structural differences (Barre et al., 2023; Sánchez‐Monge et al., 2000).…”

“…Despite its increasing popularity, mango has been identified as a significant allergen in various studies. Consumption of mango can lead to allergic reactions that range from mild symptoms to severe and potentially life‐threatening anaphylaxis (Barre et al., 2023; Honglei & Yanjun, 2024). Mango allergy can manifest in two types of hypersensitivity reactions: Type I and Type IV.…”