Abstract
Enzyme-linked immunosorbent assays (ELISAs) are widely used to determine gluten contamination in gluten-free and low gluten food samples. ELISA assays developed using monoclonal antibodies against known toxic peptides have an advantage in the identification of toxic prolamin content in protein extracts of different food samples, as well as raw materials. R5 and G12 monoclonal antibodies specific for two known toxic peptides used in commercially available gluten ELISA assays were applied to test toxic peptide contents in wheat relatives and wild wheat species with different genome composition and complexity. Although the R5 peptide content showed some correlation with ploidy levels in Triticum species, there was a high variance among Aegilops species. Some of the analysed diploid Aegilops species showed extremely high R5 peptide contents. Based on the bioinformatics analyses, the R5 peptide was present in most of the sulphur rich prolamins in all the analysed species, whereas the G12 epitope was exclusively present in alpha gliadins. High variation was detected in the position and frequency of epitopes in sequences originating from the same species, thus highlighting the importance of genotypic variation within species. Identification of new prolamin alleles of wheat relatives and wild wheat species is of great importance in order to find germplasm for special end-use quality purposes as well as development of food with reduced toxicity.
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Amano, M., Ogawa, H., Kojima, K., Kamidaira, T., Suetsugu, S., Yoshihama, M., Satoh, T., Samejima, T., Matsumoto, I. 1998. Identification of the major allergens in wheat flour responsible for baker’s asthma. Biochem. J. 330:1229–1234.
Anderson, R.P., Degano, P., Godkin, A.J., Jewell, D.P., Hill, A.V.S. 2000. In vivo antigen challenge in celiac disease identifies a single transglutaminase-modified peptide as the dominant A gliadin T-cell epitope. Nature (Med) 6:337–342.
Anderson, R.P., Wieser, H. 2006. Medical applications of gluten-composition knowledge. In: Wrigley, C.W., Békés, F., Bushuk, W. (eds), Gliadin and Glutenin. In: The Unique Balance of Wheat Quality. AACCI Press. St. Paul, MN, USA, pp. 387–409.
Armentia, A., Martin-Santos, J.M., Blanco, M. 1990. Exercise induced anaphylaxis reaction to grain flows. Ann. Allergy 65:149–151.
Breiteneder, H., Radauer, C. 2004. A classification of plant food allergens. J. Allergy Clin. Immunol. 113:821–830.
Camarca, A., Anderson, R.P., Mamone, G., Fierro, O., Facchiano, A., Costantini, S., Zanzi, D., Sidney, J., Auricchio, S., Sette, A., Troncone, R., Gianfrani, C. 2009. Intestinal T cell responses to gluten peptides are largely heterogeneous: Implications for a peptide-based therapy in celiac disease. J. Immunol. 182:4158–4166.
Catassi, C., Fasano, A. 2008. Celiac disease. In: Arendt, E.K., Dal Bello, F. (eds), Gluten-Free Cereal Products and Beverages. Academic Press, San Diego, CA, USA, pp. 1–28.
Clarke, B.C., Appels, R. 1999. Sequence variation at the Sec-1 locus of rye, Secale cereale (Poaceae). Plant Syst. Evol. 214:1–14.
Codex Standard for Foods for Special Dietary Use for Persons Intolerant to Gluten — CODEX STAN 118 — 1979, adopted in 1979; amended in 1983; revised in 2008, Codex Alimentarius, International Food Standards. Rome, Italy.
Farkas, A., Molnár, I., Dulai, S., Rapi, S., Oldal, V., Cseh, A., Kruppa, K., Molnár-Láng, M. 2014. Increased micronutrient content (Zn, Mn) in the 3Mb (4B) wheat — Aegilops biuncialis substitution and 3Mb.4BS translocation identified by GISH and FISH. Genome 57:61–67.
Juhász, A., Gell, Gy., Sebestyén, E., Haraszi, R., Tamás, L., Balázs, E. 2012a. Brachypodium distachyon as a model for defining the allergen potential of non-prolamin proteins. Funct. Integr. Genomics 12:439–446.
Juhász, A., Gell, Gy., Békés, F., Balázs, E. 2012b. The epitopes in wheat proteins for defining toxic units relevant to human health. Funct. Integr. Genomics 12:585–598.
Laurièrre, M., Pecquet, C., Bouchez-Mahiout, I., Snegaroff, J., Bayrou, O., Raison-Peyron, N., Vigan, M. 2006. Hydrolyzed wheat proteins present in cosmetics can induce immediate hypersensitivities. Contact Dermatitis 54:283–289.
Mills, E.N.C., Madsen, C., Shewry, P.R., Wichers, H.J. 2003. Food allergens of plant origin — their molecular and evolutionary relationships. Trends in Food Sci. Technol. 14:145–156.
Molberg, O., Uhlen, A.K., Jensen, T., Flaete, N.S., Fleckenstein, B., Arentz-Hansen, H., Raki, M., Lundin, K.E., Sollid, L.M. 2005. Mapping of gluten T-cell epitopes in the bread wheat ancestors: implications for celiac disease. Gastroenterology 128:393–401.
Morón, B., Cebolla, Á., Manyani, H., Álvarez-Maqueda, M., Megías, M., Thomas, M. del C., López, M.C., Sousa, C. 2008. Sensitive detection of cereal fractions that are toxic to celiac disease patients by using monoclonal antibodies to a main immunogenic wheat peptide. Am. J. Clin. Nutr. 87:405–414.
Osman, A.A., Uhlig, H.H., Valdes, I., Amin, M., Mendez, E., Mothes, T. 2001. A monoclonal antibody that recognizes a potential coeliac-toxic repetitive pentapeptide epitope in gliadins. Eur. J. Gastroent. Hepatol. 13:1189–1193.
Radauer, C., Breiteneder, H. 2007. Evolutionary biology of plant food allergens. J. Allergy Clin. Immun. 120:518–525.
Sampson, H.A., Metcalfe, D.D. 1992. Food allergies. J. Amer. Med. Assoc. 268:2840–2844.
Santra, M., Matthews, S.B., Thompson, H.J. 2013. Development of a core collection of Triticum and Aegilops species for improvement of wheat for activity against chronic diseases. Agriculture and Food Security 2:4.
Sapone, A., Bai, J.C., Ciacci, C., Dolinsek, J., Green, P.H.R., Hadjivassiliou, M., Kaukinen, K., Rostami, K., Sanders, D.S., Schumann, M., Ullrich, R., Villalta, D., Volta, U., Catassi, C., Fasano, A. 2012. Spectrum of gluten-related disorders: Consensus on new nomenclature and classification. BMC Medicine 10:13.
Schneider, A., Molnár, I., Molnár-Láng, M. 2008. Utilisation of Aegilops (goatgrass) species to widen the genetic diversity of cultivated wheat. Euphytica 163:1–19.
Skerritt, J.H., Lew, P.H., Castle, L.S. 1988. Accumulation of gliadin and glutenin polypeptides during development of normal and sulphur-deficient wheat seed: Analysis using specific monoclonal antibodies. J. Exp. Bot. 39:723–737.
Sollid, L.M., Qiao, S.W., Anderson, R.P., Gianfrani, C., Koning, F. 2012. Nomenclature and listing of celiac disease relevant gluten T-cell epitopes restricted by HLA-DQ molecules. Immunogenetics 64:455–460.
Valdés, I., García, E., Llorente, M., Méndez, E. 2003. Innovative approach to low-level gluten determination in foods using a novel sandwich enzyme-linked immunosorbent assay protocol. Eur. J. Gastroenterol. 15:465–474.
van Herpen, T.W.J.M., Goryunova, S.V., van der Schoot, J., Mitreva, M., Salentijn, E.M.J., Vorst, O., Schenk, M.F., van Veelen, P.A., Koning, F., van Soest, L.J.M., Vosman, B., Bosch, D., Hamer, R.J., Gilissen, L.J.W.J., Smulders, M.J.M. 2006. Alpha-gliadin genes from the A, B, and D genomes of wheat contain different sets of celiac disease epitopes. BMC Genomics 7:1.
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Gell, G., Kovács, K., Molnár, I. et al. Celiac Disease-Specific Prolamin Peptide Content of Wheat Relatives and Wild Species Determined by ELISA Assays and Bioinformatics Analyses. CEREAL RESEARCH COMMUNICATIONS 43, 133–143 (2015). https://doi.org/10.1556/CRC.43.2015.1.13
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DOI: https://doi.org/10.1556/CRC.43.2015.1.13