Cross-Reaction between Gliadin and Different Food and Tissue Antigens

Abstract

A subgroup of coeliac disease patients continues to experience symptoms even on a gluten-free diet (GFD). We attempted to determine whether these symptoms could be due to either cross-contamination with gluten-containing foods or cross-reactivity between α-gliadin and non-gluten foods consumed on a GFD. We measured the reactivity of affinity-purified polyclonal and monoclonal α-gliadin 33-mer peptide antibodies against gliadin and additional food antigens commonly consumed by patients on a GFD using ELISA and dot-blot. We also examined the immune reactivity of these antibodies with various tissue antigens. We observed significant immune reactivity when these antibodies were applied to cow's milk, milk chocolate, milk butyrophilin, whey protein, casein, yeast, oats, corn, millet, instant coffee and rice. To investigate whether there was cross-reactivity between α-gliadin antibody and different tissue antigens, we measured the degree to which this antibody bound to these antigens. The most significant binding occurred with asialoganglioside, hepatocyte, glutamic acid decarboxylase 65, adrenal 21-hydroxylase, and various neural antigens. The specificity of anti-α-gliadin binding to different food and tissue antigens was demonstrated by absorption and inhibition studies. We also observed significant cross-reactivity between α-gliadin 33-mer and various food antigens, but some of these reactions were associated with the contamination of non-gluten foods with traces of gluten. The consumption of cross-reactive foods as well as gluten-contaminated foods may be responsible for the continuing symptoms presented by a subgroup of patients with coeliac disease. The lack of response of some CD patients may also be due to antibody cross-reactivity with non-gliadin foods. These should then be treated as gluten-like peptides and should also be excluded from the diet when the GFD seems to fail.

Correlation of Tissue Antibodies and Food Immune Reactivity in Randomly Selected Patient Specimens

“…While CD researcher's state there is no test for NCGS [42][43][44], others are boldly defining steps to differentiating CD from NCGS [45][46][47][48]. Indeed Vojdani and Tarash [15] show the affinity for gliadin antibodies to bind to human tissue beyond the gut, which can lead to autoimmunity. Interestingly, the gluten-free diet (GFD) is generally recommended for specific autoimmune disorders, as the GFD may reduce systemic inflammation, cut down on the frequency of flares, or arrest the autoantibody production against targeted tissues [49][50][51][52].…”

“…the mechanism of food contributing to autoimmunity via antibody cross-reactivity. In an earlier study, Vojdani and Tarash [15] found significant cross-reactivity between gliadin antibody and multiple human tissues including: asialoganglioside, cytochrome P450, glutamic acid decarboxylase 65, 21 hydroxylase, myelin basic protein, cerebellar, osteocyte, synapsin, myocardial peptide, ovary, thyroid peroxidase.…”

“…In this study we investigated the prevalence of specific food protein antibodies made simultaneously with human tissue antibodies. The food groups included here are gluten family protein antibodies and dairy family protein antibodies, both of which have been shown to cross-react with human tissues [14][15][16][17] and finally, food lectins and agglutinins, which are known to bind to human tissues [18,19]. the mechanism of food contributing to autoimmunity via antibody cross-reactivity.…”

Detection of antibodies against human and plant aquaporins in patients with multiple sclerosis

“…It is possible that exposure to epitopes that resemble human AQP4 from exogenous sources such as plants may play a role in the etiology of RRMS and possibly other autoimmune disorders. Although an association between plant antigens and autoimmune diseases has been previously suggested for celiac disease, lupus, scleroderma, type I diabetes, and MS [40][41][42][43][44], there is need for further evaluation of the role of plant proteins in the generation of cross-reactive antibodies against human AQP4, S100B, MOG, and MBP and the consequent development of RRMS and other neuroimmune disorders. This may help in the development of dietary guidelines for dietary modifications for patients with neuroimmune disorders.…”

The Occurrence of Sequences Identical with Epitopes from the Allergen Pen a 1.0102 Among Food and Non-Food Proteins

“…Fragments similar to celiac-toxic peptides were found in, among others, sequences of bovine -casein, maize prolamin, oat and yeast proteins [Darewicz et al, 2007]. The presence of the above fragments can be considered as the molecular basis of cross-reactivity between the above--mentioned proteins and wheat gliadins [Cabrera-Chávez & Calderón de la Barca, 2009; Cabrera-Chávez et al, 2012; Vojdani & Tarash, 2013] studied in vitro using antibodies from celiac patients. In the case of arthropod tropomyosins the consensus sequence constitutes allergenic region [Marti et al, 2007].…”