Gluten, Celiac Disease, and Gluten Intolerance and the Impact of Gluten Minimization Treatments with Prolylendopeptidase on the Measurement of Gluten in Beer

Literature Cited

• Ajith, A., Labuschagne, M. T., Malan, A. F., van Biljon, A., and Wentzel, B. Relationship between malting quality traits and hordeins as affected by timing of nitrogen fertilizer application. Cereal Chem. 87:393–397, 2010.
   Web of Science ®Google Scholar
• Alvarez, P. A., Mongeon, V. J., and Boye, J. I. Characterization of a gluten reference material: Wheat-contaminated oats. J. Cereal Sci. 57:418–423, 2013.
   Web of Science ®Google Scholar
• Anderson, R., Henry, M., Taylor, R., Duncan, E., Danoy, P., Costa, M., Addison, K., Tye-Din, J., Kotowicz, M., Knight, R., Pollock, W., Nicholson, G., Toh, B.-H., Brown, M., and Pasco, J. A novel serogenetic approach determines the community prevalence of celiac disease and informs improved diagnostic pathways. BMC Med. 11:188, 2013.
   PubMed Web of Science ®Google Scholar
• Anderson, R. P., Degano, P., Godkin, A. J., Jewell, D. P., and Hill, A. V. S. In vivo antigen challenge in celiac disease identifies a single transglutaminase-modified peptide as the dominant A-gliadin T-cell epitope. Nat. Med. 6:337–342, 2000.
   PubMed Web of Science ®Google Scholar
• Anderson, R. P., Heel, D. A. v., Tye-Din, J. A., Barnardo, M., Salio, M., Jewell, D. P., and Hill, A. V. S. T-cells in peripheral blood after gluten challenge in coeliac disease. Gut 54:1217–1223, 2005.
   PubMed Web of Science ®Google Scholar
• Anderson, R. P., Jewell, D. P., and Hill, A. V. Peripheral blood T cells induced by gluten challenge in coeliac disease target a specific molecular motif and express a gut-homing integrin. Gastroenterology 120:A684, 2001.
   Web of Science ®Google Scholar
• Arentz-Hansen, E. H., McAdam, S. N., Molberg, O., Kristiansen, C., and Sollid, L. M. Production of a panel of recombinant gliadins for the characterisation of T cell reactivity in coeliac disease. Gut 46:46–51, 2000.
   PubMed Web of Science ®Google Scholar
• Arentz-Hansen, H., Korner, R., Molberg, O., Quarsten, H., Vader, W., Kooy, Y. M. C., Lundin, K. E. A., Koning, F., Roepstorff, P., Sollid, L. M., and McAdam, S. N. The intestinal T cell response to alpha-gliadin in adult celiac disease is focused on a single deamidated glutamine targeted by tissue transglutaminase. J. Exp. Med. 191:603–612, 2000.
   PubMed Web of Science ®Google Scholar
• Armstrong, M. J., Hegade, V. S., and Robins, G. Advances in coeliac disease. Curr. Opin. Gastroenterol. 28:104–112, 2012.
   Web of Science ®Google Scholar
• Aubrecht, E., and Biacs, P. A. Characterization of buckwheat grain proteins and its products. Acta Aliment. 30:71–80, 2001.
   Web of Science ®Google Scholar
• Australian Food News. Global gluten-free market set to grow. http://www.ausfoodnews.com.au/2010/07/13/global-gluten-free-market-set-to-grow.html
   Google Scholar
• Ballabio, C., Uberti, F., Di Lorenzo, C., Brandolini, A., Penas, E., and Restani, P. Biochemical and immunochemical characterization of different varieties of amaranth (Amaranthus L. ssp.) as a safe ingredient for gluten-free products. J. Agric. Food Chem. 59:12969–12974, 2011.
   Web of Science ®Google Scholar
• Beissbarth, T., Tye-Din, J. A., Smyth, G. K., Speed, T. P., and Anderson, R. P. A Systematic approach for comprehensive t-cell epitope discovery using peptide libraries. Bioinformatics 21:I29–I37, 2005.
   Web of Science ®Google Scholar
• Belton, P. S., Delgadillo, I., Halford, N. G., and Shewry, P. R. Kafirin structure and functionality. J. Cereal Sci. 44:272–286, 2006.
   Web of Science ®Google Scholar
• Bethune, M. T., and Khosla, C. In: Methods in Enzymology, Vol. 502: Protein Engineering for Therapeutics, Pt A. K. D. Wittrup and G. L. Verdine, Eds. Elsevier, San Diego, CA. Pp. 241–271, 2012.
   Google Scholar
• Biagi, F., Campanella, J., and Corazza, G. R. Follow up on celiac disease and the communion wafer. Nutr. Rev. 62:491, 2004.
   Web of Science ®Google Scholar
• Biagi, F., Campanella, J., Martucci, S., Pezzimenti, D., Ciclitira, P. J., Ellis, H. J., and Corazza, G. R. A milligram of gluten a day keeps the mucosal recovery away: A case report. Nutr. Rev. 62:360–363, 2004.
   PubMed Web of Science ®Google Scholar
• Biesiekierski, J. R., Newnham, E. D., Irving, P. M., Barrett, J. S., Haines, M., Doecke, J. D., Sheperd, S. J., Muir, J. G., and Gibson, P. R. Gluten causes gastrointestinal symptoms in subjects without coeliac disease: A double-blind randomised placebo-controlled trial. Am. J. Gastroenterol. 106:508–514, 2010.
   Web of Science ®Google Scholar
• Biesiekierski, J. R., Peters, S. L., Newnham, E. D., Rosella, O., Muir, J. G., and Gibson, P. R. No effects of gluten in patients with self-reported non-celiac gluten sensitivity following dietary reduction of low-fermentable, poorly-absorbed, short-chain carbohydrates. Gastroenterology 145:320–328, 2013.
   PubMed Web of Science ®Google Scholar
• Bordusa, F., and Jakubke, H.-D. The specificity of prolyl endopeptidase from Flavobacterium meningoseptum: Mapping the S' subsites by positional scanning via acyl transfer. Bioorg. Med. Chem. 6:1775–1780, 1998.
   Web of Science ®Google Scholar
• Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of dye binding. Anal. Chem. 72:248–254, 1976.
   Google Scholar
• Breddam, K., and Sorensen, S. B. Isolation of carboxypeptidase III from malted barley by affinity chromatography. Carslberg Res. Commun. 52:275–283, 1987.
   Google Scholar
• Breddam, K., Sorensen, S. B., and Ottesen, M. Isolation of carboxypeptidase II from malted barley by affinity chromatography. Carslberg Res. Commun. 50:199–209, 1985.
   Google Scholar
• Brett, G. M., Mills, E. N. C., Parmar, S., Tatham, A. S., Shewry, P. R., and Morgan, M. R. A. Monoclonal antibodies that recognize the repeat motif of the S-poor prolamins. J. Cereal Sci. 12:245–255, 1990.
   Web of Science ®Google Scholar
• Brown, A. C. Gluten sensitivity: Problems of an emerging condition separate from celiac disease. Expert Rev. Gastroenterol. Hepatol. 6:43–55, 2012.
   PubMed Web of Science ®Google Scholar
• Brusic, V., Bajic, V. B., and Petrovsky, N. Computational methods for prediction of T-cell epitopes—a framework for modelling, testing, and applications. Methods 34:436–443, 2004.
   PubMed Web of Science ®Google Scholar
• Bucci, C., Zingone, F., Russo, I., Morra, I., Tortora, R., Pogna, N., Scalia, G., Iovino, P., and Ciacci, C. Gliadin does not induce mucosal inflammation or basophil activation in patients with non-celiac gluten sensitivity. Clin. Gastroenterol. Hepatol. 11:1294–1299, 2013.
   PubMed Web of Science ®Google Scholar
• Bugyi, Z., Török, K., Hajas, L., Adonyi, Z., Popping, B., and Tömösközi, S. Comparative study of commercially available gluten ELISA kits using an incurred reference material. Qual. Assur. Saf. Crops Foods 5:79–87, 2013.
   Web of Science ®Google Scholar
• Bugyi, Z., Török, K., Hajas, L., Adonyi, Z., Poms, R. E., Popping, B., Diaz-Amigo, C., Kerbach, S., and Tömösközi, S. Development of incurred reference material for improving conditions of gluten quantification. J. AOAC Int. 95:382–387, 2012.
   Web of Science ®Google Scholar
• Cabrera-Chavez, F., Iametti, S., Miriani, M., de la Barca, A. M. C., Mamone, G., and Bonomi, F. Maize prolamins resistant to peptictryptic digestion maintain immune-recognition by IgA from some celiac disease patients. Plant Foods Hum. Nutr. 67:24–30, 2012.
   Web of Science ®Google Scholar
• Camarca, A., Anderson, R. P., Mamone, G., Fierro, O., Facchiano, A., Costantini, S., Zanzi, D., Sidney, J., Auricchio, S., Sette, A., Troncone, R., and Gianfrani, C. Intestinal T cell responses to gluten peptides are largely heterogeneous: Implications for a peptide-based therapy in celiac disease. J. Immunol. 182:4158–4166, 2009.
   PubMed Web of Science ®Google Scholar
• Catassi, C., Fabiani, E., Iacono, G., D'agate, C., Francavilla, R., Biagi, F., Volta, U., Accomando, S., Picarelli, A., De Vitis, I., Pianelli, G., Gesuita, R., Carle, F., Mandolesi, A., Bearzi, I., and Fasano, A. A prospective, double-blind, placebo-controlled trial to establish a safe gluten threshold for patients with celiac disease. Am. J. Clin. Nutr. 85:160–166, 2007.
   PubMed Web of Science ®Google Scholar
• Catassi, C., Fabiani, E., Ratsch, I. M., Coppa, G. V., Giorgi, P. L., Pierdomenico, R., Alessandrini, S., Iwanejko, G., Domenici, R., Mei, E., Miano, A., Marani, M., Bottaro, G., Spina, M., Dotti, M., Montanelli, A., Barbato, M., Viola, F., Lazzari, R., Vallini, M., Guariso, G., Plebani, M., Cataldo, F., Traverso, G., Ughi, C., Chiaravalloti, G., Baldassarre, M., Scarcella, P., Bascietto, F., Ceglie, L., Valenti, A., Paolucci, P., Caradonna, M., Bravi, E., and Ventura, A. The coeliac iceberg in Italy. A multicentre antigliadin antibodies screening for coeliac disease in school-age subjects. Acta Paediatr. 85:29–35, 1996.
   Web of Science ®Google Scholar
• Catassi, C., Ratsch, I. M., Fabiani, E., Ricci, S., Bordicchia, F., Pierdomenico, R., and Giorgi, P. L. High prevalence of undiagnosed celiac disease in 5280 Italian students screened by antigoliadin antibodies. Acta Paediatr. 84:672–676, 1995.
   PubMed Web of Science ®Google Scholar
• Catassi, C., Ratsch, I. M., Fabiani, E., Rossini, M., Bordicchia, F., Candela, F., Coppa, G. V., and Giorgi, P. L. Celiac-disease in the year 2000—exploring the iceberg. Lancet 343:200–203, 1994.
   PubMed Web of Science ®Google Scholar
• Chambers, S. J., Brett, G. M., Mills, E. N. C., Morgan, M. R. A. Multiantigenic peptides as standards in immunoassays for complex proteins: Use of LGQQQPFPPQQPY in an enzyme-linked immunosorbent assay for gluten. Anal. Biochem. 292:301–305, 2001.
   Web of Science ®Google Scholar
• Codex Alimentarius. http://www.codexalimentarius.net/web/index_en.jsp, 2012.
   Google Scholar
• Colgrave, M. L., Goswami, H., Howitt, C. A., and Tanner, G. J. Proteomics as a tool to understand the complexity of beer. Food. Res. Int. 54:1001–1012, 2013.
   Web of Science ®Google Scholar
• Colgrave, M. L., Goswami, H., H owitt, C. A., and Tanner, G. J. What is in a beer? Proteomic characterization and relative quantification of hordein (gluten) in beer. J. Proteome Res. 11:386–396, 2012.
   PubMed Web of Science ®Google Scholar
• Comino, I., Real, A., de Lourdes Moreno, M., Montes, R., Cebolla, ?., and Sousa, C. Immunological determination of gliadin 33-mer equivalent peptides in beers as a specific and practical analytical method to assess safety for celiac patients. J. Sci. Food Agric. 93:933–943, 2013.
   Web of Science ®Google Scholar
• Costea, M., Brenner, D. M., Tardif, F. J., Tan, Y. F., and Sun, M. Delimitation of Amaranthus cruentus L. and Amaranthus caudatus L. using micromorphology and AFLP analysis: An application in germplasm identification. Genet. Resour. Crop Evol. 53:1625–1633, 2006.
   Web of Science ®Google Scholar
• Crooks, G. E., Hon, G., Chandonia, J. M., and Brenner, S. E. WebLogo: A sequence logo generator. Genome Res. 14:1188–1190, 2004.
   PubMed Web of Science ®Google Scholar
• Daldegan, F., Rocher, A., Cameronmills, V., and Vonwettstein, D. The expression of serine carboxypeptidases during maturation and germination of the barley-grain. Proc. Natl. Acad. Sci. USA 91:8209–8213, 1994.
   Web of Science ®Google Scholar
• Davy, A., Sorensen, M. B., Svendsen, I., Cameron-Mills, V., and Simpson, D. J. Prediction of protein cleavage sites by the barley cysteine endoproteases ep-a and ep-b based on the kinetics of synthetic peptide hydrolysis. Plant Physiol. 122:137–145, 2000.
   Web of Science ®Google Scholar
• Davy, A., Svendsen, I., Sorensen, S. O., Sorensen, M. B., Rouster, J., Meldal, M., Simpson, D. J., and Cameron-Mills, V. Substrate specificity of barley cysteine endoproteases EP-A and EP-B. Plant Physiol. 117:255–261, 1998.
   Web of Science ®Google Scholar
• De Mesa-Stonestreet, J. N., Alavi, S., and Bean, S. R. Sorghum proteins: The concentration, isolation, modification, and food applications of kafirins. J. Food Sci. 75:R90–R104, 2010.
   PubMed Web of Science ®Google Scholar
• De Re, V., Caggiari, L., Tabuso, M., and Cannizzaro, R. The versatile role of gliadin peptides in celiac disease. Clin. Biochem. 46:552–560, 2013.
   Web of Science ®Google Scholar
• Diaz-Amigo, C., and Popping, B. Gluten current status and new analytical developments in support of the regulatory requirements. J. AOAC Int. 95:335–336, 2012.
   Web of Science ®Google Scholar
• Diaz-Amigo, C., and Popping, B. Labeling regulations, detection methods, and assay validation. J. AOAC Int. 95:337–348, 2012.
   PubMed Web of Science ®Google Scholar
• Diaz-Amigo, C., and Popping, B. Accuracy of ELISA detection methods for gluten and reference materials: A realistic assessment. J. Agric. Food Chem. 61:5681–5688, 2013.
   PubMed Web of Science ®Google Scholar
• Di Cagno, R., Barbato, M., Di Camillo, C., Rizzello, C. G., De Angelis, M., Giuliani, G., De Vincenzi, M., Gobbetti, M., and Cucchiara, S. Gluten-free sourdough wheat baked goods appear safe for young celiac patients: A pilot study. J. Pediatr. Gastroenterol. Nutr. 51:777–783, 2010.
   PubMed Web of Science ®Google Scholar
• Di Cagno, R., De Angelis, M., Auricchio, S., Greco, L., Clarke, C., De Vincenzi, M., Giovannini, C., D'archivio, M., Landolfo, F., Parrilli, G., Minervini, F., Arendt, E., and Gobbetti, M. Sourdough bread made from wheat and nontoxic flours and started with selected lactobacilli is tolerated in celiac sprue patients. Appl. Environ. Microbiol. 70:1088–1096, 2004.
   PubMed Web of Science ®Google Scholar
• Dicke, W. K., Weijers, H. A., and Kamer, J. H. v. D. Coeliac disease II. The presence in wheat of a factor having a deleterious effect in the causes of coeliac disease. Acta Paediatr. 42:34–42, 1953.
   PubMedGoogle Scholar
• Dostalek, P., Gabrovska, D., Rysova, J., Mena, M. C., Hernando, A., Mendez, E., Chmelik, J., and Salplachta, J. Determination of gluten in glucose syrups. J. Food Compos. Anal. 22:762–765, 2009.
   Web of Science ®Google Scholar
• Dostalek, P., Hochel, I., Mendez, E., Hernando, A., and Gabrovska, D. Immunochemical determination of gluten in malts and beers. Food Addit. Contam. 23:1074–1078, 2006.
   PubMed Web of Science ®Google Scholar
• Edens, L., Dekker, P., van der Hoeven, R., Deen, F., de Roos, A., and Floris, R. Extracellular prolyl endoprotease from Aspergillus niger and its use in the debittering of protein hydrolysates. J. Agric. Food Chem. 53:7950–7957, 2005.
   PubMed Web of Science ®Google Scholar
• Edens, L., van der Laan, J. M., and Craig, H. D. Mechanisms and prevention by proline-specific proteases. Brauwelt Int. 3:157–162, 2005.
   Google Scholar
• Ehren, J., Moron, B., Martin, E., Bethune, M. T., Gray, G. M., and Khosla, C. A food-grade enzyme preparation with modest gluten detoxification properties. PLoS One 4:e6313, 2009.
   PubMed Web of Science ®Google Scholar
• Fleckenstein, B., Molberg, Y., Qiao, S. W., Schmid, D. G., Von Der Mullbe, F., Elgstoen, K., Jung, G., and Sollid, L. M. Gliadin T cell epitope selection by tissue transglutaminase in celiac disease—role of enzyme specificity and pH influence on the transamidation versus deamidation reactions. J. Biol. Chem. 277:34109–34116, 2002.
   PubMed Web of Science ®Google Scholar
• Fontanini, D., and Jones, B. L. SEP-1—a subtilisin-like serine endopeptidase from germinated seeds of Hordeum vulgare L. cv. Morex. Planta 215:885–893, 2002.
   Web of Science ®Google Scholar
• Fowell, A. J., Thomas, P. W., Surgenor, S. L., and Snook, J. A. The epidemiology of coeliac disease in East Dorset 1993–2002: An assessment of the ‘coeliac iceberg’, and preliminary evidence of case clustering. QJM Int. J. Med. 99:453–460, 2006.
   PubMed Web of Science ®Google Scholar
• Gallagher, E., Gormley, T. R., and Arendt, E. K. Recent advances in the formulation of gluten-free cereal-based products. Trends Food Sci. Technol. 15:143–152, 2004.
   Web of Science ®Google Scholar
• Gass, J., and Khosla, C. Prolyl endopeptidases. Cell. Mol. Life Sci. 64:345–355, 2007.
   PubMed Web of Science ®Google Scholar
• Gass, J., Vora, H., Bethune, M. T., Gray, G. M., and Khosla, C. Effect of barley endoprotease EP-B2 on gluten digestion in the intact rat. J. Pharmacol. Exp. Ther. 318:1178–1186, 2006.
   PubMed Web of Science ®Google Scholar
• Gass, S. J., Bethune, M. T., Siegel, M., Spencer, A., and Khosla, C. Combination enzyme therapy for gastric digestion of dietary gluten in patients with celiac sprue. Gastroenterology 133:472–480, 2007.
   PubMed Web of Science ®Google Scholar
• Gellrich, C., Schieberle, P., and Wieser, H. Biochemical characterisation and quantification of the storage protein (secalin) types in rye flour. Cereal Chem. 80:102–109, 2003.
   Web of Science ®Google Scholar
• Gianfrani, C., Auricchio, S., and Troncone, R. Adaptive and innate immune responses in celiac disease. Immunol. Lett. 99:141–145, 2005.
   PubMed Web of Science ®Google Scholar
• Gordon, S. R., Stanley, E. J., Wolf, S., Toland, A., Wu, S. J., Hadidi, D., Mills, J. H., Baker, D., Pultz, I. S., and Siegel, J. B. Computational design of an alpha-gliadin peptidase. J. Am. Chem. Soc. 134:20513–20520, 2012.
   PubMed Web of Science ®Google Scholar
• Greco, L., Gobbetti, M., Auricchio, R., Di Mase, R., Landolfo, F., Paparo, F., Di Cagno, R., De Angelis, M., Rizzello, C. G., Cassone, A., Terrone, G., Timpone, L., D'Aniello, M., Maglio, M., Troncone, R., and Auricchio, S. Safety for patients with celiac disease of baked goods made of wheat flour hydrolyzed during food processing. Clin. Gastroenterol. Hepatol. 9:24–29, 2011.
   PubMed Web of Science ®Google Scholar
• Green, P. H. R. Mortality in celiac disease, intestinal inflammation, and gluten sensitivity. J. Am. Med. Assoc. 302:1225–1226, 2009.
   Web of Science ®Google Scholar
• Green, P. H. R., Rostami, K., and Marsh, M. N. Diagnosis of coeliac disease. Best Pract. Res. Clin. Gastroenterol. 19:389–400, 2005.
   PubMed Web of Science ®Google Scholar
• Guerdrum, L. J., and Bamforth, C. W. Levels of gliadin in commercial beers. Food Chem. 129:1783–1784, 2011.
   Web of Science ®Google Scholar
• Guerdrum, L. J., and Bamforth, C. W. Prolamin levels through brewing and the impact of prolyl endoproteinase. J. Am. Soc. Brew. Chem. 70:35–38, 2012.
   Web of Science ®Google Scholar
• Haas-Lauterbach, S., Immer, U., Richter, M., and Oehler, E. Gluten fragment detection with a competitive ELISA. J. AOAC Int. 95:377–381, 2012.
   PubMed Web of Science ®Google Scholar
• Hadjivassiliou, M., Grunewald, R. A., Kandler, R. H., Chattopadhyay, A. K., Jarratt, J. A., Sanders, D. S., Sharrack, B., Wharton, S. B., and Davies-Jones, G. A. B. Neuropathy associated with gluten sensitivity. J. Neurol. Neurosurg. Psych. 77:1262–1266, 2006.
   PubMed Web of Science ®Google Scholar
• Halbmayr-Jech, E., Hammer, E., Fielder, R., Coutts, J., Rogers, A., and Cornish, M. Characterization of G12 sandwich ELISA, a next-generation immunoassay for gluten toxicity. J. AOAC Int. 95:372–376, 2012.
   Web of Science ®Google Scholar
• Hartmann, G., Koehler, P., and Wieser, H. Rapid degradation of gliadin peptides toxic for coeliac disease patients by proteases from germinating cereals. J. Cereal Sci. 44:368–371, 2006.
   Web of Science ®Google Scholar
• Hausch, F., Shan, L., Santiago, N. A., Gray, G. M., and Khosla, C. Intestinal digestive resistance of immunodominant gliadin peptides. Am. J. Physiol. Gastrointest. Liver Physiol. 283:G996–G1003, 2002.
   PubMed Web of Science ®Google Scholar
• Hill, A. S., and Skerritt, J. H. Determination of gluten in foods using a monoclonal antibody based competition enzyme immunoassay. Food. Agric. Immun. 2:21–35, 1990.
   Google Scholar
• Hollen, E., Hogberg, L., Stenhammar, L., Falth-Magnusson, K., and Magnusson, K. E. Antibodies to oat prolamines (avenins) in children with coeliac disease. Scand. J. Gastroenterol. 38:742–746, 2003.
   PubMed Web of Science ®Google Scholar
• Inomata, N. Wheat allergy. Curr. Opin. Allergy Clin. Immunol. 9:238–243, 2009.
   PubMed Web of Science ®Google Scholar
• Ivarsson, A. The Swedish epidemic of coeliac disease explored using an epidemiological approach—some lessons to be learnt. Best Pract. Res. Clin. Gastroenterol. 19:425–440, 2005.
   PubMed Web of Science ®Google Scholar
• Jin, B., Li, L., Feng, Z. C., Li, B., Liu, G. Q., and Zhu, Y. K. Investigation of the relationship of malt protein and beer haze by proteome analysis. J. Food Process. Preserv. 36:169–175, 2012.
   Web of Science ®Google Scholar
• Jones, B. L. Endoproteases of barley and malt. J. Cereal Sci. 42:139–156, 2005.
   Web of Science ®Google Scholar
• Juhasz, A., Gell, G., Bekes, F., and Balazs, E. The epitopes in wheat proteins for defining toxic units relevant to human health. Funct. Integr. Genomics 12:585–598, 2013.
   Web of Science ®Google Scholar
• Juhasz, A., Gell, G., Sebestyen, E., Haraszi, R., Tamas, L., and Balazs, E. Brachypodium distachyon as a model for defining the allergen potential of non-prolamin proteins. Funct. Integr. Genomics 12:439–446, 2012.
   Web of Science ®Google Scholar
• Juhasz, T., Szeltner, Z., and Polgar, L. Properties of the prolyl oligopeptidase homologue from Pyrococcus furiosus. FEBS Lett. 580:3493–3497, 2006.
   PubMed Web of Science ®Google Scholar
• Kahlenberg, F., Sanchez, D., Lachmann, I., Tuckova, L., Tlaskalova, H., Mendez, E., and Mothes, T. Monoclonal antibody R5 for detection of putatively coeliac-toxic gliadin peptides. Eur. Food Res. Technol. 222:78–82, 2006.
   Web of Science ®Google Scholar
• Kamer, J. H. v., Weijers, H. A., and Dicke, W. K. Coeliac disease. IV. An investigation into the injurious constituents of wheat in connection with their action on patients with coeliac disease. Acta Paediatr. 42:223–231, 1953.
   Google Scholar
• Kasarda, D. D. Can an increase in celiac disease be attributed to an increase in the gluten content of wheat as a consequence of wheat breeding? J. Agric. Food Chem. 61:1155–1159, 2013.
   PubMed Web of Science ®Google Scholar
• Kasarda, D. D., and D'ovidio, R. Deduced amino acid sequence of an alpha-gliadin gene from spelt wheat (spelta) includes sequences active in celiac disease. Cereal Chem. 76:548–551, 1999.
   Web of Science ®Google Scholar
• Kent, P. S. Is going gluten free the next fad diet? J. Renal Nutr. 23:e47–e50, 2013.
   Web of Science ®Google Scholar
• Kim, C. Y., Quarsten, H., Bergseng, E., Khosla, C., and Sollid, L. M. Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac disease. Proc. Natl. Acad. Sci. USA 101:4175–4179, 2004.
   PubMed Web of Science ®Google Scholar
• Kiss, Z., Vecseri-Hegyes, B., Kun-Farkas, G., and Hoschke, A. Optimisastion of malting and mashing processes for the production of gluten-free beers. Acta Aliment. 40:67–78, 2011.
   Web of Science ®Google Scholar
• Larre, C., Lupi, R., Gombaud, G., Brossard, C., Branlard, G., Moneret-Vautrin, D. A., Rogniaux, H., and Denery-Papini, S. Assessment of allergenicity of diploid and hexaploid wheat genotypes: Identification of allergens in the albumin/globulin fraction. J. Proteomics 74:1279–1289, 2011.
   PubMed Web of Science ®Google Scholar
• Lastovickova, M., Mazanec, K., Benkovska, D., and Bobalova, J. Utilization of the linear mode of MALDI-TOF mass spectrometry in the study of glycation during the malting process. J. Inst. Brew. 116:245–250, 2011.
   Web of Science ®Google Scholar
• Leffler, D., Schuppan, D., Pallav, K., Najarian, R., Goldsmith, J. D., Hansen, J., Kabbani, T., and Dennis, M. Kinetics of the histological, serological and symptomatic responses to gluten challenge in adults with coeliac disease. Gut 62:996–1004, 2013.
   PubMed Web of Science ®Google Scholar
• Lopez, M., and Edens, L. Effective prevention of chill-haze in beer using an acid proline-specific endoprotease from Aspergillus niger. J. Agric. Food Chem. 53:7944–7949, 2005.
   Web of Science ®Google Scholar
• Mamone, G., Ferranti, P., Melck, D., Tafuro, F., Longobardo, L., Chianese, L., and Addeo, F. Susceptibility to transglutaminase of gliadin peptides predicted by a mass spectrometry-based assay. FEBS Lett. 562:177–182, 2004.
   PubMed Web of Science ®Google Scholar
• Marti, T., Molberg, O., Li, Q., Gray, G. M., Khosla, C., and Sollid, L. M. Prolyl endopeptidase-mediated destruction of T cell epitopes in whole gluten: Chemical and immunological characterization. J. Pharmacol. Exp. Ther. 312:19–26, 2005.
   PubMed Web of Science ®Google Scholar
• Marttila, S., Jones, B. L., and Mikkonen, A. differential localisation of 2 acid proteinases in germinating barley (Hordeum vulgare) seed. Physiol. Plant. 93:317–327, 1995.
   Web of Science ®Google Scholar
• Matysiak-Budnik, T., Candalh, C., Cellier, C., Dugave, C., Namane, A., Vidal-Martinez, T., Cerf-Bensussan, N., and Heyman, M. Limited efficiency of prolyl-endopeptidase in the detoxification of gliadin peptides in celiac disease. Gastroenterology 129:786–796, 2005.
   PubMed Web of Science ®Google Scholar
• Mena, M. C., Lombarda, M., Hernando, A., Mendez, E., and Albar, J. P. Comprehensive analysis of gluten in processed foods using a new extraction method and a competitive ELISA based on the R5 antibody. Talanta 91:33–40, 2012.
   PubMed Web of Science ®Google Scholar
• Mendez, E., Vela, C., Immer, U., and Janssen, F. W. Report of a collaborative trial to investigate the performance of the r5 enzyme linked immunoassay to determine gliadin in gluten-free food. Eur. J. Gastroenterol. Hepatol. 17:1053–1063, 2005.
   PubMed Web of Science ®Google Scholar
• Mickowska, B., Socha, P., Urminská, D., and Cieślik, E. Immunodetection, electrophoresis and amino acid composition of alcohol soluble proteins extracted from grains of selected varieties of pseudocereals, legumes, oat, maize and rice. Cereal Res. Commun. 41:160–169, 2013.
   Web of Science ®Google Scholar
• Mills, E. N. C., Field, J. M., Kauffman, J. A., Tatham, A. S., Shewry, P. R., and Morgan, M. R. A. Characterization of a monoclonal antibody specific for HMW subunits of glutenin and its use to investigate glutenin polymers. J. Agric. Food Chem. 48:611–617, 2000.
   Web of Science ®Google Scholar
• Mitea, C., Havenaar, R., Drijfhout, J. W., Edens, L., Dekking, L., and Koning, F. Efficient degradation of gluten by a prolyl endoprotease in a gastrointestinal model: Implications for coeliac disease. Gut 57:25–32, 2006.
   Web of Science ®Google Scholar
• Pastorello, E. A., Farioli, L., Conti, A., Pravettoni, V., Bonomi, S., Iametti, S., Fortunato, D., Scibilia, J., Bindslev-Jensen, C., Ballmer-Weber, B., Robino, A. M., and Ortolani, C. Wheat IgE-mediated food allergy in European patients: Alpha-amylase inhibitors, lipid transfer proteins and low-molecular-weight glutenins—allergenic molecules recognized by double-blind, placebo-controlled food challenge. Int. Arch. Allergy Immunol. 144, 10–22, 2007.
   PubMed Web of Science ®Google Scholar
• Perrocheau, L., Rogniaux, H., Boivin, P., and Marion, D. Probing heat-stable, water-soluble proteins from barley to malt and beer. Proteomics 5:2849–2858, 2005.
   PubMed Web of Science ®Google Scholar
• Picarelli, A., Di Tola, M., Sabbatella, L., Gabrielli, F., Di Cello, T. E., Anania, M. C., Mastracchio, A., Silano, M., and De Vincenzi, M. Immunologic evidence of no harmful effect of oats in celiac disease. Am. J. Clin. Nutr. 74:137–140, 2001.
   PubMed Web of Science ®Google Scholar
• Piper, J. L., Gray, G. M., and Khosla, C. Effect of prolyl endopeptidase on digestive-resistant gliadin peptides in vivo. J. Pharmacol. Exp. Ther. 311:213–219, 2004.
   PubMed Web of Science ®Google Scholar
• Pontieri, P., Mamone, G., De Caro, S., Tuinstra, M. R., Roemer, E., Okot, J., De Vita, P., Ficco, D. B. M., Alifano, P., Pignone, D., Massardo, D. R., and Del Giudice, L. Sorghum, a healthy and gluten-free food for celiac patients as demonstrated by genome, biochemical, and immunochemical analyses. J. Agric. Food Chem. 61:2565–2571, 2013.
   PubMed Web of Science ®Google Scholar
• Pyle, G. G., Paaso, B., Anderson, B. E., Allen, D. D., Marti, T., Li, Q., Siegel, M., Khosla, C., and Gray, G. M. Effect of pretreatment of food gluten with prolyl endopeptidase on gluten-induced malabsorption in celiac sprue. Clin. Gastroenterol. Hepatol. 3:687–694, 2005.
   PubMed Web of Science ®Google Scholar
• Real, A., Comino, I., de Lorenzo, L., Merchan, F., Gil-Humanes, J., Gimenez, M. J., Lopez-Casado, M. A., Torres, M. I., Cebolla, A., Sousa, C., Barro, F., and Piston, F. Molecular and immunological characterization of gluten proteins isolated from oat cultivars that differ in toxicity for celiac disease. PLoS One 7:e48365, 2012.
   Web of Science ®Google Scholar
• Rechinger, K. B., Bougri, O. V., and Cameron-Mills, V. Evolutionary relationship of the members of the sulphur-rich hordein family revealed by common antigenic determinants. Theor. Appl. Genet. 85:829–840, 1993.
   Web of Science ®Google Scholar
• Rizzello, C. G., De Angelis, M., Di Cagno, R., Camarca, A., Silano, M., Losito, A., De Vincenzi, M., De Bari, M. D., Palmisano, F., Maurano, F., Gianfrani, C., and Gobbetti, M. Highly efficient gluten degradation by lactobacilli and fungal proteases during food processing: New perspectives for celiac disease. Appl. Environ. Microbiol. 73:4499–4507, 2007.
   PubMed Web of Science ®Google Scholar
• Rumbo, M., Margheritis, A. I., Chirdo, F. G., Giorgieri, S. A., Fossati, C. A., and Anon, M. C. Fractionation of secalins and hordeins by preparative electrophoresis at acid pH. Eur. Food Res. Technol. 214:198–201, 2002.
   Web of Science ®Google Scholar
• Sapone, A., Bai, J. C., Ciacci, C., Dolinsek, J., Green, P. H. R., Hadjivassiliou, M., Kaukinen, K., Rostami, K., D.S., S., Schumann, M., Ullrich, R., Villalta, D., Volta, U., Catassi, C., and Fasano, A. Spectrum of gluten-related disorders: Consensus on new nomenclature and classification. Biomed. Central Med. 10:13, 2012.
   Google Scholar
• Shan, L., Martin, T., Sollid, L. M., Gray, G. M., and Khosla, C. Comparative biochemical analysis of three bacterial prolyl endopeptidases: Implications for coeliac sprue. Biochem. J. 383:311–318, 2004.
   PubMed Web of Science ®Google Scholar
• Shan, L., Mathews, I., and Khosla, C. Structural and mechanistic analysis of two prolyl endopeptidases: Role of interdomain dynamics in catalysis and specificity. Proc. Natl. Acad. Sci. USA 102:3599–3604, 2005.
   PubMed Web of Science ®Google Scholar
• Shan, L., Molberg, O., Parrot, I., Hausch, F., Filiz, F., Gray, G. M., Sollid, L. M., and Khosla, C. Structural basis for gluten intolerance in celiac sprue. Science 297:2275–2279, 2002.
   PubMed Web of Science ®Google Scholar
• Shan, L., Qiao, S. W., Arentz-Hansen, H., Molberg, O., Gray, G. M., Sollid, L. M., and Khosla, C. Identification and analysis of multivalent proteolytically resistant peptides from gluten: Implications for celiac sprue. J. Proteome Res. 4:1732–1741, 2005.
   PubMed Web of Science ®Google Scholar
• Shang, H. Y., Wei, Y. M., Long, H., Yan, Z. H., and Zheng, Y. L. Identification of LMW glutenin-like genes from Secale sylvestre host. Russ. J. Genet. 41:1372–1380, 2005.
   Web of Science ®Google Scholar
• Sharma, G. M. Immunoreactivity and detection of wheat proteins by commercial ELISA kits. J. AOAC Int. 95:364–371, 2012.
   Web of Science ®Google Scholar
• Shewry, P. R. Avenins: The prolamins of oats. In: Seed Proteins P. R. Shewry and R. Casey, Eds. Klewer: London. Pp. 79–92, 1999.
   Google Scholar
• Shewry, P. R., Halford, N. G., Belton, P. S., and Tatham, A. S. The structure and properties of gluten: An elastic protein from wheat grain. Philos. Trans. R. Soc. Lond. Ser. B Biol. Sci. 357:133–142, 2002.
   PubMed Web of Science ®Google Scholar
• Shewry, P. R., Tatham, A. S., and Halford, N. G. In: Seed Proteins. P. R. Shewry and R. Casey, Eds. Klewer: London. Pp. 35–78, 1999.
   Google Scholar
• Shigemitsu, T., Saito, Y., Morita, S., and Satoh, S., Masumura, T. Separation and identification of rice prolamins by two-dimensional gel electrophoresis and amino acid sequencing. Biosci. Biotechnol. Biochem. 76:594–597, 2012.
   PubMed Web of Science ®Google Scholar
• Siegel, M., Bethune, M. T., Gass, J., Ehren, J., Xia, J., Johannsen, A., Stuge, T. B., Gray, G. M., Lee, P. P., and Khosla, C. Rational design of combination enzyme therapy for celiac sprue. Chem. Biol. 13:649–658, 2006.
   PubMed Web of Science ®Google Scholar
• Simpson, D. J. Proteolytic degradation of cereal prolamins—the problem with proline. Plant Sci. 161:825–838, 2001.
   Web of Science ®Google Scholar
• Skerritt, J. H., and Hill, A. S. Enzyme-immunoassay for determination of gluten in foods—collaborative study. J. Assoc. Off. Anal. Chem. 74:257–264, 1991.
   PubMedGoogle Scholar
• Skerritt, J. H., Hill, A. S., and Andrews, J. L. Antigenicity of wheat prolamins: Detailed epitope analysis using a panel of monoclonal antibodies. J. Cereal Sci. 32:259–279, 2000.
   Web of Science ®Google Scholar
• Skovbjerg, H., Tarnow, L., Locht, H., and Parving, H. H. The prevalence of coeliac disease in adult Danish patients with type 1 diabetes with and without nephropathy. Diabetologia 48:1416–1417, 2005.
   PubMed Web of Science ®Google Scholar
• Sollid, L. M., Arentz-Hansen, H., Fleckenstein, B., Lundin, K. E. A., McAdam, S., Molberg, O., Qiao, S. W., and Quarsten, H. The T Cell Response to Gluten and Control of Coeliac Disease Development. In: Coeliac Disease: Proceedings of the Xth International Symposium on Coeliac Disease, Paris. John Libbey Eurotext, Esher, UK, 2003.
   Google Scholar
• Sollid, L. M., Molberg, O., McAdam, S., and Lundin, K. E. A. Autoantibodies in coeliac disease: Tissue transglutaminase—guilt by association? Gut 41:851–852, 1997.
   PubMed Web of Science ®Google Scholar
• Sollid, L. M., Qiao, S. W., Anderson, R. P., Gianfrani, C., and Koning, F. Nomenclature and listing of celiac disease relevant gluten T-cell epitopes restricted by HLA-DQ molecules. Immunogenetics 64:455–460, 2012.
   PubMed Web of Science ®Google Scholar
• Song, R., Llaca, V., Linton, E., and Messing, J. Sequence, regulation, and evolution of the maize 22-kD alpha-Zein gene family. Genome Res. 11:1817–1825., 2001.
   PubMed Web of Science ®Google Scholar
• Srinivasan, U., Jones, E., Carolan, J., and Feighery, C. Immunohistochemical analysis of coeliac mucosa following ingestion of oats. Clin. Exp. Immunol. 144:197–203, 2006.
   PubMed Web of Science ®Google Scholar
• Stenman, S. M., Venalainen, J. I., Lindfors, K., Auriola, S., Mauriala, T., Kaukovirta-Norja, A., Jantunen, A., Laurila, K., Qiao, S., Sollid, L. M., Mannisto, P. T., Kaukinen, K., and Maki, M. Enzymatic detoxification of gluten by germinating wheat proteases: Implications for new treatment of celiac disease. Ann. Med. 41:390–400, 2009.
   PubMed Web of Science ®Google Scholar
• Stepniak, D., Koning, F. Celiac disease—sandwiched between innate and adaptive immunity. Hum. Immunol. 67:460–468, 2006.
   PubMed Web of Science ®Google Scholar
• Stepniak, D., Spaenij-Dekking, L., Mitea, C., Moester, M., de Ru, A., Baak-Pablo, R., van Veelen, P., Edens, L., and Koning, F. Highly efficient gluten degradation with a newly identified prolyl endoprotease: Implications for celiac disease. Am. J. Physiol. Gastrointest. Liver Physiol. 291:G621–G629, 2006.
   PubMed Web of Science ®Google Scholar
• Storsrud, S., Olsson, M., Lenner, R. A., Nilsson, L. A., Nilsson, O., and Kilander, A. Adult coeliac patients do tolerate large amounts of oats. Eur. J. Clin. Nutr. 57:163–169, 2003.
   PubMed Web of Science ®Google Scholar
• Tanner, G. J., Blundell, M. J., Colgrave, M. L., and Howitt, C. A. Quantification of hordeins by ELISA: The correct standard makes a magnitude of difference. PLoS One 8:e56456, 2013.
   PubMed Web of Science ®Google Scholar
• Tanner, G. J., Colgrave, M. L., Blundell, M. J., Goswami, H. P., and Howitt, C. A. Measuring Hordein (Gluten) in Beer. A comparison of ELISA and mass spectrometry. PLoS One 8:e56452, 2013.
   Web of Science ®Google Scholar
• Tanner, G. J., Howitt, C. A., Forrester, R. I., Campbell, P. M., Tye-Din, J. A., and Anderson, R. P. Dissecting the T-cell response to hordeins in coeliac disease can develop barley with reduced immunotoxicity. Aliment. Pharmacol. Ther. 32:1184–1191, 2010.
   PubMed Web of Science ®Google Scholar
• Tatham, A. S., Fido, R. J., Moore, C. M., Kasarda, D. D., Kuzmicky, D. D., Keen, J. N., and Shewry, P. R. Characterisation of the major orolamins of tef (Eragrostis tef) and finger millet (Eleusine coracana). J. Cereal Sci. 24:65–71, 1996.
   Web of Science ®Google Scholar
• Tatham, A. S., and Shewry, P. R. The S-poor prolamins of wheat, barley and rye. J. Cereal Sci. 22:1–16, 1995.
   Web of Science ®Google Scholar
• Tatham, A. S., and Shewry, P. R. Allergens in wheat and related cereals. Clin. Exp. Allergy 38:1712–1726, 2008.
   PubMed Web of Science ®Google Scholar
• Terp, N., Thomsen, K. K., Svendsen, I., Davy, A., and Simpson, D. J. Purification and characterization of hordolisin, a subtilisin-like serine endoprotease from barley. J. Plant Physiol. 156:468–476, 2000.
   Web of Science ®Google Scholar
• Tye-Din, J. A., Anderson, R. P., French, R. A., Brown, G. J., Hodsman, P., Siegel, M., Botwick, W., and Shreeniwas, R. The effects of ALV003 pre-digestion of gluten on immune response and symptoms in celiac disease in vivo. Clin. Immunol. 134:289–295, 2010.
   PubMed Web of Science ®Google Scholar
• Tye-Din, J. A., Stewart, J. A., Dromey, J. A., T., B., van Heel, D. A., Tatham, A., Henderson, K., Mannering, S. I., Gianfrani, C., Derek, P. Jewell, D. P., Hill, A. V. S., McCluskey, J., Jamie Rossjohn, J., and Anderson, R. P. Comprehensive, quantitative mapping of T cell epitopes in gluten in celiac disease. Sci. Translational Med. 2:41ra51, 2010.
   PubMed Web of Science ®Google Scholar
• Ulbricht, C., Chao, W., Nummy, K., Rusie, E., Tanguay-Colucci, S., Iannuzzi, C. M., Plammoottil, J. B., Varghese, M., and Weissner, W. Chia (Salvia hispanica): A systematic review by the natural standard research collaboration. Rev. Recent Clin. Trials 4:168–174, 2009.
   Google Scholar
• Vader, L. W., de Ru, A., van der Wal, Y., Kooy, Y. M. C., Benckhuijsen, W., Mearin, M. L., Drijfhout, J. W., van Veelen, P., and Koning, F. Specificity of tissue transglutaminase explains cereal toxicity in celiac disease. J. Exp. Med. 195:643–649, 2002.
   PubMed Web of Science ®Google Scholar
• Vader, W., Kooy, Y., Van Veelen, P., De Ru, A., Harris, D., Benckhuijsen, W., Pena, S., Mearin, L., Drijfhout, J. W., and Koning, F. The gluten response in children with celiac disease is directed toward multiple gliadin and glutenin peptides. Gastroenterology 122:1729–1737, 2002.
   PubMed Web of Science ®Google Scholar
• Wieser, H., and Koehler, P. Detoxification of gluten by means of enzymatic treatment. J. AOAC Int. 95:356–363, 2012.
   Web of Science ®Google Scholar
• Wild, D., Robins, G. G., Burley, V. J., and Howdle, P. D. Evidence of high sugar intake, and low fibre and mineral intake, in the gluten-free diet. Aliment. Pharmacol. Ther. 32:573–581, 2010.
   PubMed Web of Science ®Google Scholar
• Xie, Z. Z., Wang, C. Y., Wang, K., Wang, S. L., Li, X. H., Zhang, Z., Ma, W. J., and Yan, Y. M. Molecular characterization of the celiac disease epitope domains in alpha-gliadin genes in Aegilops tauschii and hexaploid wheats (Triticum aestivum L.). Theor. Appl. Genet. 121:1239–1251, 2010.
   Web of Science ®Google Scholar
• Zar, S., Benson, M. J., and Kumar, D. Food-specific serum IgG4 and IgE titers to common food antigens in irritable bowel syndrome. Am. J. Gastroenterol. 100:1550–1557, 2005.
   PubMed Web of Science ®Google Scholar
• Zevallos, V. F., Ellis, H. J., Suligoj, T., Herencia, L. I., and Ciclitira, P. J. Variable activation of immune response by quinoa (Chenopodium quinoa Willd.) prolamins in celiac disease. Am. J. Clin. Nutr. 96:337–344, 2012.
   PubMed Web of Science ®Google Scholar
• Zhang, N., and Jones, B. L. Development of proteolytic activities during barley malting and their localization in the green malt kernel. J. Cereal Sci. 22:147–155, 1995.
   Web of Science ®Google Scholar
• Zuo, X. L., Li, Y. Q., Li, W. J., Guo, Y. T., Lu, X. F., Li, J. M., and Desmon, P. V. Alterations of food antigen-specific serum immunoglobulins G and E antibodies in patients with irritable bowel syndrome and functional dyspepsia. Clin. Exp. Allergy 37:823–830, 2007.
   PubMed Web of Science ®Google Scholar