RESEARCH PAPER
Antibody reactivity in patients with IgE-mediated wheat allergy to various subunits and fractions of gluten and non-gluten proteins from ω-gliadin-free wheat genotypes
 
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1
Institute of Biology, Pedagogical University of Cracow, Kraków, Poland
2
Department of Clinical and Environmental Allergology, Collegium Medicum, Jagiellonian University, Kraków, Poland
3
Plant Breeding and Acclimatization Institute – National Research Institute, Radzików, Poland
CORRESPONDING AUTHOR
Iwona Stawoska   

Institute of Biology, Pedagogical University of Cracow, Kraków, Poland
 
Ann Agric Environ Med. 2017;24(2):229–236
KEYWORDS
ABSTRACT
Introduction and objective:
Gluten proteins (gliadins and glutenins) are polymorphic wheat storage proteins of allergenic properties. Significant differences in chemical composition between both protein groups allow to expect highly specific immunological response of individual subunits and fractions in reactions with IgE sera of people allergic to wheat. The aim of these studies was to identify and characterize the most allergenic gluten proteins (GP) and nongluten proteins (NGP) occurred in two closely related wheat hybrid genotypes.

Material and Methods:
3xC and 3xN wheat hybrids, which differ strongly in regard of gliadin composition, were analyzed. Seven people manifesting different symptoms of wheat allergy donated sera for the experiment. The technique of immunoblotting after SDS-PAGE was used for identification of allergenic subunits and fractions among GP and NGP. Immunologically active protein bands were visualized by chemiluminescence.

Results:
Great variation of immunodetection spectra was observed. Results of immunoblotting showed LMW glutenins to be of highest, gliadins of medium, while NGP of lowest allergenicity for selected patients. The 43-kDa and 47-kDa LMW glutenin subunits, 40-kDa and 43-kDa γ-gliadin fractions and 49-kDa NGP can be considered as the most immunoreactive among all protein bands [b]separated by SDS-PAGE.

Conclusions:
The observed differentiation of immunodetection spectra allows to model highly specific IgE-binding profiles of allergenic wheat proteins attributed to individual patients with symptoms of gluten intolerance. Highly immunoreactive subunits and fractions among GP and NGP were identified. The observed immunoreactivity of 49 kDa NGP is worth to emphasize, as it has never been reported as wheat allergenic protein before.

 
REFERENCES (36)
1.
Wrigley C, Békés F, Bushuk W. Gluten: A balance of gliadin and glutenin. In: Wrigley C, Békés F, Bushuk W, editors. Gliadin and glutenin. The unique balance of wheat quality. Minnesota, USA; AACC International, St Paul; 2006. p. 3–32.
 
2.
Metakovsky E, Graybosch R. Gliadin alleles in wheat: identification and applications. In: Wrigley C, Békés F, Bushuk W, editors. Gliadin and Glutenin: The Unique Balance of Wheat Quality. Minnesota, USA; AACC International, St Paul; 2006. p. 85–114.
 
3.
Payne PI. Genetics of Wheat Storage Proteins and the Effect of Allelic Variation on Bread-Making Quality. Annu Rev Plant Physiol. 1987; 38(1): 141–153.
 
4.
Sozinov A, Poperelya F. Genetic classification of prolamines and its use for plant breeding. Ann Techn Agric. 1980; 29(2): 229–245.
 
5.
Metakovsky E, Gomez M, Vazquez J, Carrillo J. High genetic diversity of Spanish common wheats as judged from gliadin alleles. Plant Breed. 2000; 119(1): 37–42.
 
6.
Dupont FM, Vensel WH, Tanaka CK, Hurkman WJ, Altenbach SB. Deciphering the complexities of the wheat flour proteome using quantitative two-dimensional electrophoresis, three proteases and tandem mass spectrometry. Proteome Sci. 2011; 9(10): 1–29.
 
7.
Shewry PR, Tatham AS, Halford NG. The prolamins of the Triticeae. In: Shewry PR, Casey R, editors. Seed proteins. Dordrecht; Springer Netherlands; 1999. p. 35–78.
 
8.
Shewry PR, Halford NG, Tatham AS, Popineau Y, Lafiandra D, Belton PS. The high molecular weight subunits of wheat glutenin and their role in determining wheat processing properties. Adv Food Nutr Res. 2003; 45: 219–302.
 
9.
Shewry P, Tatham A. Disulphide bonds in wheat gluten proteins. J Cereal Sci. 1997; 25(3): 207–227.
 
10.
Bonomi F, Iametti S, Mamone G, Ferranti P. The Performing Protein: Beyond Wheat Proteomics? Cereal Chem. 2013; 90(4): 358–366.
 
11.
Tanabe S. Identification of wheat allergens. Internet Symposium Food Allergens. 2001; 3(4): 163–170.
 
12.
Tatham AS. The structures of wheat proteins. In: Schofield JD, Editor. Wheat Structure: Biochemistry and Functionality. Cambridge, UK; The Royal Society of Chemistry; 1996. p. 53–62.
 
13.
Köhler P, Belitz H-D, Wieser H. Disulphide bonds in wheat gluten: further cystine peptides from high molecular weight (HMW) and low molecular weight (LMW) subunits of glutenin and from γ-gliadins. Zeitschrift für Lebensmittel-Untersuchung und Forschung. 1993; 196(3): 239–247.
 
14.
Tanabe S, Arai S, Yanagihara Y, Mita H, Takahashi K, Watanabe M. A major wheat allergen has a Gln-Gln-Gln-Pro-Pro motif identified as an IgE-binding epitope. Biochem Biophys Res Commun. 1996; 219(2): 290–293.
 
15.
Aalberse RC, Crameri R. IgE-binding epitopes: a reappraisal. Allergy. 2011; 66(10): 1261–1274.
 
16.
Palosuo K, Varjonen E, Kekki O-M, Klemola T, Kalkkinen N, Alenius H, et al. Wheat ω-5 gliadin is a major allergen in children with immediate allergy to ingested wheat. J Allergy Clin Immunol. 2001; 108(4): 634–638.
 
17.
Morita E, Yamamura Y, Mihara S, Kameyoshi Y, Yamamoto S. Food-dependent exercise-induced anaphylaxis: a report of two cases and determination of wheat-γ-gliadin as the presumptive allergen. Br J Dermatol. 2000; 143(5): 1059–1063.
 
18.
Jacquenet S, Morisset M, Battais F, Denery-Papini S, Croizier A, Baudouin E, et al. Interest of immunoCAP system to recombinant ω-5 gliadin for the diagnosis of exercise-induced wheat allergy. Int Arch Allergy Immunol. 2009; 149(1): 74–80.
 
19.
Lauriere M, Pecquet C, Boulenc E, Bouchez-Mahiout I, Snegaroff J, Choudat D, et al. Genetic differences in omega-gliadins involved in two different immediate food hypersensitivities to wheat. Allergy. 2007; 62(8): 890–896.
 
20.
Snégaroff J, Branlard G, Bouchez-Mahiout I, Laudet B, Tylichova M, Chardot T, et al. Recombinant proteins and peptides as tools for studying IgE reactivity with low-molecular-weight glutenin subunits in some wheat allergies. J Agric Food Chem. 2007; 55(24): 9837–9845.
 
21.
Battais F, Mothes T, Moneret-Vautrin DA, Pineau F, Kanny G, Popineau Y, et al. Identification of IgE-binding epitopes on gliadins for patients with food allergy to wheat. Allergy. 2005; 60(6): 815–821.
 
22.
Battais F, Pineau F, Popineau Y, Aparicio C, Kanny G, Guerin L, et al. Food allergy to wheat: identification of immunogloglin E and immunoglobulin G-binding proteins with sequential extracts and purified proteins from wheat flour. Clin Exp Allergy. 2003; 33(7): 962–970.
 
23.
Kusaba-Nakayama M, Ki M, Iwamoto M, Shibata R, Sato M, Imaizumi K. CM3, one of the wheat α-amylase inhibitor subunits, and binding of IgE in sera from Japanese with atopic dermatitis related to wheat. Food Chem Toxicol. 2000; 38(2): 179–185.
 
24.
Zapatero L, Martinez M, Alonso E, Salcedo G, Sánchez-Monge R, Barber D, et al. Oral wheat flour anaphylaxis related to wheat α-amylase inhibitor subunits CM3 and CM16. Allergy. 2003; 58(9): 955–960.
 
25.
Waga J, Skoczowski A. Development and characteristics of ω-gliadin-free wheat genotypes. Euphytica. 2014; 195(1): 105–116.
 
26.
Curioni A, Dal Belin Peruffo A, Pressi G, Pogna N. Immunological distinction between x-type and y-type high molecular weight glutenin subunits. Cereal Chem. 1991; 68(2): 200–204.
 
27.
Skoczowski A, Obtułowicz K, Czarnobilska E, Dyga W, Stachowicz M, Waga J. Patient-dependent differentiation of gluten protein IgE-binding epitopes in wheat allergy. Przegl Lek [Medical Review]. 2012; 70(12): 1043–1047.
 
28.
Waga J, Obtułowicz K, Zientarski J, Czarnobilska E, Skoczowski A. Purified Wheat Gliadin Proteins as Immunoglobulin E Binding Factors in Wheat Mediated Allergies. Am J Plant Sci. 2011; 2(03): 476–483.
 
29.
Varjonen E, Vainio E, Kalimo K. Antigliadin IgE–indicator of wheat allergy in atopic dermatitis. Allergy. 2000; 55(4): 386–391.
 
30.
Klockenbring T, Boese A, Bauer R, Goerlich R. Comparative investigations of wheat and spelt cultivars: IgA, IgE, IgG1 and IgG4 binding characteristics. Food Agric Immunol. 2001; 13(3): 171–181.
 
31.
Maruyama N, Ichise K, Katsube T, Kishimoto T, Kawase Si, Matsumura Y, et al. Identification of major wheat allergens by means of the Escherichia coli expression system. Eur J Biochem. 1998; 255(3): 739–745.
 
32.
Matsuo H, Dahlström J, Tanaka A, Kohno K, Takahashi H, Furumura M, et al. Sensitivity and specificity of recombinant ω-5 gliadin-specific IgE measurement for the diagnosis of wheat-dependent exercise-induced anaphylaxis. Allergy. 2008; 63(2): 233–236.
 
33.
Bouchez-Mahiout I, Snégaroff J, Tylichova M, Pecquet C, Branlard G, Laurière M. Low Molecular Weight Glutenins in Wheat-Dependant, Exercise-Induced Anaphylaxis: Allergenicity and Antigenic Relationships with Omega 5-Gliadins. Int Arch Allergy Immunol. 2010; 153(1): 35–45.
 
34.
Hofmann S, Fischer J, Eriksson C, Bengtsson Gref O, Biedermann T, Jakob T. IgE detection to α/β/γ-gliadin and its clinical relevance in wheat-dependent exercise-induced anaphylaxis. Allergy. 2012; 67(11): 1457–1460.
 
35.
Ito K, Futamura M, Borres MP, Takaoka Y, Dahlstrom J, Sakamoto T, et al. IgE antibodies to ω-5 gliadin associate with immediate symptoms on oral wheat challenge in Japanese children. Allergy. 2008; 63(11): 1536–1542.
 
36.
Sanchez-Monge R, Garcia-Casado G, Armentia A, Salcedo G. Wheat flour peroxidase is a prominent allergen associated with baker’s asthma. Clin Exp Allergy. 1997; 27(10): 1130–1137.
 
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