Null Alleles in Gliadin Coding Loci and Wheat Allergenic Properties


Wheat gliadin proteins-an important, nutritional component of many food products may also act as allergenic proteins causing various, clinical symptoms of IgE-mediated food allergies. Gliadins are coded by six complex loci on the chromosomes 1A, 1B, 1D,6A, 6B and 6D of wheat genome. Each of the loci coding from a few to a dozen of polypeptides may spontaneously mutate to inactive gene variants called null alleles that do not code any proteins at all. The aim of the present work was to find out whether null alleles in some gliadin coding loci may decrease wheat allergenic properties. Six winter wheat genotypes: gliadin deletion lines (GDL) containing null alleles on 1D, 1B and 6B chromosomes and control lines (CL) containing active gene variants in all gliadin coding loci, were developed using plant breeding methods. Allergenic properties of the six analyzed hybrids were estimated by ELISA using polled sera of five patients allergic to gluten. Estimated immunoreactivity of GDLs was from 6% to 18% lower as compared with CLs. The obtained results evidenced that gliadin null alleles decrease wheat allergenic properties and may be used as parental forms for breeding of hypoallergenic wheat genotypes.

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J. Waga, J. Zientarski, M. Szaleniec, K. Obtułowicz, W. Dyga and A. Skoczowski, "Null Alleles in Gliadin Coding Loci and Wheat Allergenic Properties," American Journal of Plant Sciences, Vol. 4 No. 1, 2013, pp. 160-168. doi: 10.4236/ajps.2013.41021.

Conflicts of Interest

The authors declare no conflicts of interest.


[1] P. R. Shewry, N. G. Halfornd, A. S. Tatham, Y. Popineau, D. Lafiandra and P. S. Belton, “The High Molecular Weight Sub-units of Wheat Glutenin and Their Role in Determining Wheat Processing Properties,” Advances in Food & Nutrition Research, Vol. 45, 2003, pp. 219-302. doi:10.1016/S1043-4526(03)45006-7
[2] H. Wieser, “Chemistry of Gliadins,” European Journal of Gastroenterology & Hepatology, Vol. 3, No. 2, 1991, pp. 102-107.
[3] H. Gall, M. Steinert and R. U. Peter, “Exercise-Induced Anaphylaxis to Wheat Flour,” Allergy, Vol. 55, No. 11, 2000, pp. 1096-1097. doi:10.1034/j.1398-9995.2000.00812.x
[4] A. S. Tatham and P. R. Shewry, “Allergens in Wheat Related Cereals,” Clinical & Experimental Allergy, Vol. 38, No. 11, 2008, pp. 1712-1726.
[5] E. V. Metakovsky, “Gliadin Allele Identification in common Wheat. II. Catalogue of Gliadin Alleles in Common Wheat,” Journal of Genetics and Breeding, Vol. 45, 1991, pp. 325-344.
[6] J. A. Bietz, “HPLC of Cereal Endosperm Storage Proteins,” In: K. M. Gooding and F. E. Regnier, Eds., HPLC of Biological Macromolecules, 2nd Edition, Marcel Dekker, Inc., New York, 2002.
[7] P. I. Payne, “Genetics of Wheat Storage Proteins and the Effect of Allelic Variation on Bread-Making Quality,” Annual Review of Plant Physiology, Vol. 38, 1987, pp. 141-152. doi:10.1146/annurev.pp.38.060187.001041
[8] S. M. Gilbert, N. Wallner, P. S. Belton, J. A. Greenfield, G. Siligardi, P. R. Shewry and A. S. Tatham, “Expression and Characterisation of a Highly Repetitive Peptide Derived from Wheat Seed Storage Proteins,” Biochimica et Biophysica Acta, Vol. 1479, No. 1-2, 2000, pp. 135-146. doi:10.1016/S0167-4838(00)00059-5
[9] A. A. Sozinov and F. A. Poperella, “Genetic Classification of Prolamins and Its Use for Plant Breeding,” Annales de Technologie Agricole, Vol. 28, 1980, pp. 229-245.
[10] A. De Bustos, P. Rubio and N. Jouve. “Molecular Characterization of the Inactive Allele of the Gene Glu A1 and the Development of a Set of AS-PCR Markers for HMW Glutenins of Wheat,” Theoretical and Applied Genetics, Vol. 100, 7, 2000, pp. 1085-1094. doi:10.1007/s001220051390
[11] O. D. Anderson and F. C. Greene, “The α-Gliadin Gene Family. II. DNA and Protein Sequence Variation, Subfamily Structure and Origins of Pseudogenes,” Theoretical and Applied Genetics, Vol. 95, No. 1-2, 1997, pp. 59-65. doi:10.1007/s001220050532
[12] G. Branlard and M. Dardevet, “A null Gli-D1 Allele with a Positive Effect on Bread Wheat Quality,” Journal of Cereal Science, Vol. 20, No. 3, 1994, pp. 235-244. doi:10.1006/jcrs.1994.1063
[13] W. J. Rogers, E. J. Sayers and K. L. Ru, “Deficiency of Individual High Molecular Glutenin Subunits Affords Flexibility in Breeding Strategies for Bread-Making Quality in Wheat Triticum aestivum L,” Euphitica, Vol. 117, No. 2, 2001, pp. 99-109. doi:10.1023/A:1004152027155
[14] S. W?grzyn and J. Waga, “Relationships between the High Molecular Weight Glutenin Subunits and Variation of the Important Useful Traits of Winter Wheat Cultivars and Strains,” Biuletyn—Instytutu Hodowli i Aklimatyzacji Roslin, Vol. 211, 1999, pp. 55-69.
[15] E. Witkowski, J. Waga, K. Witkowska, M. Rapacz, M. Gut, A. Bielawska, H. Luber and A. J. Lukaszewski, “Association be-tween Frost Tolerance and the Allele of High Molecular Weight Glutenin Subunits Present in Polish Winter Wheats,” Euphytica, Vol. 159, No. 3, 2008, pp. 377-384. doi:10.1007/s10681-007-9537-9
[16] J. Waga, “Catalogue of Gliadin Protein Blocks Occurring in Polish Common Wheat Cultivars and Strains (Triticum aestivum L.),” Bi-uletyn—Instytutu Hodowli i Aklimatyzacji Roslin, Vol. 243, 2007, pp. 3-23.
[17] J. Waga, J. Zientarski, M. Szaleniec and A. Skoczowski, “Efficiency of Poroshell Type Chromatographic Columns for Wheat Gliadin Separation Using RP-HPLC,” Biuletyn—Instytutu Hodowli i Aklimatyzacji Roslin, Vol. 260-261, 2011, pp. 5-20.
[18] J. Waga, J. Zientarski, K. Obtu?owicz and B. Bilo, “Flour Quality and Binding of Immunoglobulin E by Gliadin Proteins of Two Winter Wheat Genotypes,” Polish Journal of Food And Nutrition Sciences , Vol. 15, No. 56, 2006, pp. 305-310.
[19] G. L. Lookhart, S. R. Bean and J. A. Bietz, “HPLC of Gluten Monomeric Proteins,” In: P. R. Shewry and G. L. Lookhart, Eds., Wheat Gluten Protein Analysis, American Association of Cereal Chemists, St. Paul, 2003, pp. 91-111.
[20] H. Wieser and P. Koehler, “The Biochemical Basis of Celiac Disease,” Cereal Chemistry, Vol. 85, No. 1, 2008, pp. 1-13. doi:10.1094/CCHEM-85-1-0001
[21] I. Bouchez-Mahiout, J. Snegaroff, M. Tylichova, C. Pecquet, G. Branlard and M. Lauriere, “Low Molecular Weight Glutennins in Wheat Dependant, Exercise-Induced Anaphylaxis: Allegenicity and Antigenic Relationships with Omega 5-Gliadins,” International Archives of Allergy and Immunology, Vol. 153, No. 1, 2010, pp. 35-45. doi:10.1159/000301577
[22] K. Palosuo, E. Varionen, O. M. Kekki, T. Klemola, N. Kalkkinen H. , Alenius and T. Reunala, “Wheat ω-5 Gliadin Is a Major Allergen in Children with Immediate Allergy to Ingested Wheat,” Journal of Allergy and Clinical Immunology, Vol. 108, No. 4, 2001, pp. 634-638. doi:10.1067/mai.2001.118602
[23] J. Waga, K. Obtu?owicz, J. Zientarski, E. Czarnobilska and A. Skoczowski, “Purified Wheat Gliadin Proteins as Immunoglobulin E Binding Factors in Wheat Mediated Allergies,” American Journal of Plant Sciences, Vol. 2, No. 3, 2011, pp. 476-483. doi:10.4236/ajps.2011.23056
[24] Y. Tada, M. Nakase, T. Adachi, R. Nakamura H. , Shimada, M. Takahashi, T. Fujimura and T. Matsuda, “Reduction of 14-16 kDa Allergenic Proteins in Transgenic rice Plants by Antisense Gene,” FEBS Letters, Vol. 391, No. 3, 1996, pp. 341-345. doi:10.1016/0014-5793(96)00773-9
[25] E. M. Herman, R. M. Helm, R. Jung and A. J. Kinney, “Genetic Modification Removes an Immunodominant Allergen from Soybean,” Plant Physiology, Vol. 132, No. 1, 2003, pp. 36-43. doi:10.1104/pp.103.021865
[26] S. B. Altenbach and P. V. Allen, “Transformation of the US Bread Wheat ‘Butte 86’ and Silencing of Omega-5 Gliadin Genes,” GM Crops, Vol. 2, No. 1, 2011, , pp. 66-73. doi:10.4161/gmcr.2.1.15884

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