The epitopes in wheat proteins for defining toxic units relevant to human health

Springer Science and Business Media LLC - Tập 12 - Trang 585-598 - 2012
Angéla Juhász1, Gyöngyvér Gell1, Frank Békés2, Ervin Balázs1
1Applied Genomics Department, Agricultural Institute, Centre for Agricultural Research, HAS, Martonvásár, Hungary
2FBFD PTY LTD, Beecroft, Australia

Tóm tắt

Wheat-related disorders are well-studied health problems. Knowledge of the composition and amounts of epitopes present in a single wheat sample represents a significant gap, and the detailed wheat proteome datasets now available can provide the necessary information to carry out an estimation of allergen prediction for a single cultivar. The combined use of genome sequence and allergen databases, prediction methodology, and cereal chemistry results in better understanding of the level of toxicity present in the end-products produced from wheat flour. The workflow presented in this review provides information about the number and distribution of epitopes at single protein, or protein fraction, levels. In addition, epitopes present in the highest frequency and harmful proteins expressed in the highest amount can be identified. The “epitope toxicity” value obtained in this way is a significant research output from the analysis of large datasets that can be applied to the food industry.

Tài liệu tham khảo

Akagawa M, Takeshi M, Shigenori I, Morita N, Suyamato K (2007) Proteomic analysis of wheat flour allergens. J Agric Food Chem 55:6863–6870 Altenbach SB, Kothari KM, Tanaka CK, Hurkman WJ (2007) Genes encoding the PR-4 protein wheatwin are developmentally regulated in wheat grains and respond to high temperatures during grainfill. Plant Sci 173:135–143 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 RP, Wieser H (2006) Medical applications of gluten—composition knowledge. In: Wrigley CW, Békés F, Bushuk W (eds) Gliadin and glutenin. The unique balance of wheat quality. AACCI Press, St Paul, pp 387–409 Anderson RP, Degano P, Godkin AJ, Jewell DP, Hill AVS (2000) In vivo antigen challenge in celiac disease identifies a single transglutaminase-modified peptid as the dominant A gliadin T-cell epitope. Nature (Med) 6:337–342 Armentia A, Martin-Santos JM, Blanco M (1990) Exercise induced anaphylaxis reaction to grain flows. Ann Allergy 65:149–151 Bredehorst R, David K (2001) What establishes a protein as an allergen? J Chromatogr B Biomed Sci Appl 756:33–40 Breiteneder H (2008) Can any protein become an allergen? Rev Fr Allergol Immunol Clin 2008(48):135–138 Breiteneder H, Radauer C (2004) A classification of plant food allergens. J Allergy Clin Immunol 113:821–830 Brusic V, Rudy G, Honeyman G, Hammer J, Harrison LC (1998) Prediction of MHC class II-binding peptides using an evolutionary algorithm and artificial neural network. Bioinformatics 14:121–130 Brusic V, Petrovsky N, Zhang G, Bajic VB (2002) Prediction of promiscuous peptides that bind HLA class I molecules. Immunol Cell Biol 80:280–285 Brusic V, Petrovsky N, Gendel SM, Millot M, Gigonzac O, Stelman SJ (2003) Computational tools for the study of allergens. Allergy 58:1083–1092 Brusic V, Bajic VB, Petrovsky N (2004) Computational methods for prediction of T-cell epitopes—a framework for modelling, testing, and applications. Methods 34(4):436–443 Catassi C, Fasano A (2008) Celiac disease. In: Arendt EK, Dal Bello F (eds) Gluten-free cereal products and beverages. Academic Press, San Diego, pp 1–28 Chou PY, Fasman GD (2006) Prediction of the secondary structure of proteins from their amino acid sequence. In: Meister A (ed) Advances in enzymology and related areas of molecular biology, vol 47. John Wiley & Sons, Inc, Hoboken Davies IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, Wang X, Murray LW, Arendall WB, Snoeyink J, Richardson JS, Richardson DC (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35:W375–W383, 10.1093/nar/gkm216 Donnes P, Elofsson A (2002) Prediction of MHC class I binding peptides, using SVMHC. BMC Bioinformatics 3:25 Doytchinova IA, Walshe V, Borrow P, Flower DR (2005) Towards the chemometric dissection of peptide-HLAA* 0201 binding affinity: comparison of local and global QSAR models. J Comput Aided Mol Des 19:203–212 Dupont FM, Vensel W, Tanaka CK, Hurkman WJ, Altenbach SB (2011) Deciphering the complexities of the wheat flour proteome using quantitative two-dimensional electrophoresis, three proteases and tandem mass spectrometry. Proteome Sci 9:10 Emini EA, Hughes JV, Perlow DS, Boger J (1985) Induction of hepatitis A virus neutralizing antibody by a virus-specific synthetic peptide. J Virol 55:836–839 Garsed K, Scott BB (2007) Can oats be taken in a gluten-free diet? A systematic review. Scand J Gastroenterol 42(2):171–178 Green PH, Cellier C (2007) Celiac disease. N Engl J Med 357:1731–1743. doi:10.1056/NEJMra071600 Henderson KN, Tye-Din JA, Reid HH, Chen Z, Borg NA, Beissbarth T, Tatham A, Mannering SI, Purcell AW, Dudek NL, van Heel DA, McCluskey J, Rossjohn J, Anderson RP (2007) A structural and immunological basis for the role of human leukocyte antigen DQ8 in celiac disease. Immunity 27:23–34 Juhász A, Gy G, Sebestyén E, Haraszi R, Tamás L, Balázs E (2012) Brachypodium distachyon as a model for defining the allergen potential of non-prolamin proteins. Funct Integr Genomics 12:439–446. doi:10.1007/s10142-012-0294-z Karplus PA, Schultz GE (1985) Prediction of chain flexibility in proteins. Naturwissenschaften 72:212–222 Kolaskar AS, Tongaonkar PC (1990) A semi-empirical method for prediction of antigenic determinants on protein antigens. FEBS Lett 276(1–2):172–174 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 MacNamara A, Kadolsky U, Bangham CRM, Asquith B (2009) T-cell epitope prediction: rescaling can mask biological variation between MHC molecules. PLoS Comput Biol 5(3):e1000327 Mills ENC, Madsen C, Shewry PR, Wichers HJ (2003) Food allergens of plant origin—their molecular and evolutionary relationships. Trends Food Sci Technol 14:145–156 Moolhuijzen P (2011) Bioinformatics approaches for functional predictions in diverse informatics environments. PhD Thesis. Murdoch University, Perth Osorio C, Wen N, Gemini R, Zemetra R, Wettstein D, Rustgi S (2012) Targeted modification of wheat grain protein to reduce the content of celiac causing epitopes. Funct Interg Genomics 12(3):417–438. doi:10.1007/s10142-012-0287-y Parker JM, Guo D, Hodges RS (1986) New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites. Biochemistry 25:5425–5432 Popineau Y, Pineau F (1988) Changes of conformation and surface hydrophobicity of gliadins. Lebensm Wiss Technol 21:113–117 Radauer C, Breiteneder H (2007) Evolutionary biology of plant food allergens. J Allergy Clin Immun 120:518–525 Rammensee H, Bachmann J, Emmerich NP, Bachor OA, Stevanović S (1999) SYFPEITHI: database for MHC ligands and peptide motifs. Immunogenetics 50:213–219 Rigetti AC, Chillemi GF (1978) Isoelectric focusing of peptides. J Chrom 156:243–251 Salcedo G, Quirce S, Diaz-Perales A (2011) Wheat allergens associated with baker’s asthma. J Investig Allergol Clin Immunol 21(2):81–92 Salentijn EMJ, Mitea DC, Goryunova SV, van der Meer IM, Padioleau I, Gilissen LJWJ, Koning F, Smulders MJM (2012) Celiac disease T-cell epitopes from gamma-gliadins: immunoreactivity depends on the genome of origin, transcript frequency, and flanking protein variation. BMC Genomics 13:277 Sampson HA, Metcalfe DD (1992) Food allergies. J Am Med Assoc 268:2840–2844 Sapone A, Bai JC, Ciacci C, Dolinsek J, Green PHR, Hadjivassiliou M, Kaukinen K, Rostami K, Sanders DS, 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 Med 10:13. doi:10.1186/1741-7015-10-13 Shan L, Molberg Ø, Parrot I, Hausch F, Filiz F, Gray GM, Sollid LM, Khosla C (2002) Structural basis for gluten intolerance in celiac sprue. Science 297(5590):2275–2279 Shewry PR, Miles MJ, Thomson NH, Tatham S (1997) Scanning probe microscopes—applications in cereal science. Cereal Chem 74:193–199 Shewry PR, D’Ovidio R, Lafiandra D, Jenkins JA, Mills NF, Békés F (2009) Wheat grain proteins. In: Khan K, Shewry PR (eds) Wheat chemistry and technology. AACC Press, St Paul, pp 223–298 Sollid LM, Qiao SW, Anderson RP, 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. doi:10.1007/s00251-012-0599-z Tal M, Silberstein A, Nusser E (1980) Why does Coomassie Brilliant Blue R interact differently with different proteins? A partial answer. Biol Chem 260:9976–9980 Tasleem-Tahir A, Nadaud I, Chambon C, Branlard G (2012) Expression profiling of starchy endosperm metabolic proteins at 21 stages of wheat grain development. J Proteome Res 11:2754–2773 Tatham AS, Shewry PR (2008) Allergens in wheat and related cereals. Clin Exp Allergy 38:1712–1726 Tomar N, De RK (2010) Immunoinformatics: an integrated scenario. Immunology 131:153–168 Van Heel DA, West J (2006) Recent advances in coeliac disease. Gut 55:1037–1046 Van Regenmortel MHV (1996) Mapping epitope structure and activity: from one-dimensional prediction to four-dimensional description of antigenic specificity. Methods 9:465–472 Vogel JP et al (2010) Genome sequencing and analysis of the model grass Brachypodium distachyon. Nature 463:763–768 Wieser H (2008) Detection of gluten. In: Arendt EK, Dal Bello F (eds) Gluten-free cereal products and beverages. Academic Press, San Diego, pp 47–80