Recombinant Proteins and Peptides as Tools for Studying IgE Reactivity with Low-Molecular-Weight Glutenin Subunits in Some Wheat Allergies

Snégaroff, Jacques; Branlard, Gérard; Bouchez-Mahiout, Isabelle; Laudet, Béatrice; Tylichová, Martina; Chardot, Thierry; Pecquet, C.; Choudat, D.; Raison‐Peyron, Nadia; Vigan, M.; Kerre, S.; Laurière, Michel

doi:10.1021/jf071432x

Cited by 21 publications

(28 citation statements)

References 31 publications

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“…These results have confirmed the immunoreactivity of α, β and γ gliadins, previously reported in our study that tested purified gliadin fractions by ELISA [28]. The current work is also consistent with the results obtained by other authors who reported allergenicity of α, β and γ gliadins in atopic dermatitis, and LMW glutenins in baker's asthma [20,29,30]. The study of Maruyama et al [31] determined their relative reactivity in the following order: glutenins>gliadins>NGP.…”

Section: Discussionsupporting

confidence: 92%

“…In turn, ω-1.2 gliadins were evidenced to be allergenic for patients with atopic dermatitis [19]. LMW glutenins play an important role in the development of immediate hypersensitivity to hydrolyzed wheat proteins (IHHWPs) baker's asthma, atopic dermatitis and EIWA [18,20]. Battais et al showed elevated levels of IgE antibodies against all GP in the sera of 28 patients with atopic dermatitis, asthma, urticaria and eczema, which suggested that these proteins were important factors contributing to disease development [21,22].…”

Section: Introductionmentioning

confidence: 99%

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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

Skoczowski¹,

Obtułowicz²,

Czarnobilska³

et al. 2017

Ann Agric Environ Med.

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Skoczowski A, Obtułowicz K, Czarnobilska E, Dyga W, Mazur M, Stawoska I, Waga J. 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. Ann Agric Environ Med. 2017; 24(2): 229-236. doi: 10.5604/12321966.1233572 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. Materials and method. 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 separated by SDS-PAGE. Conclusion. 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.

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Section: Discussionsupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

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

Skoczowski¹,

Obtułowicz²,

Czarnobilska³

et al. 2017

Ann Agric Environ Med.

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“…LMW-GS B16 and P73 have been previously described [15]. They can be considered as models for LMW-GS coded by wheat genomes B and D, respectively.…”

Section: Resultsmentioning

confidence: 99%

“…One gene called A12 was obtained. The cloning of the two recombinant LMW-GS, called LMW-GS B16 and P73, has already been described [15]. …”

Section: Methodsmentioning

confidence: 99%

“…Among glutenins, HMW-GS have been identified as major allergens in the Japanese population suffering from WDEIA [10]. LMW-GS have been identified as IgE-reacting proteins for food allergies to wheat [11,12,13], including WDEIA [14,15]. It is interesting to note that, while ω5-gliadins and LMW-GS were both detected by ELISA and immunoblotting as major IgE-reacting proteins in WDEIA, this was not the case when an in vitro mast cell degranulation test was used.…”

Section: Introductionmentioning

confidence: 99%

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Low Molecular Weight Glutenins in Wheat-Dependant, Exercise-Induced Anaphylaxis: Allergenicity and Antigenic Relationships with Omega 5-Gliadins

Bouchez-Mahiout

Snégaroff

Tylichová

et al. 2010

Int Arch Allergy Immunol

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Background: Adults suffering from wheat-dependant, exercise-induced anaphylaxis (WDEIA) develop IgE directed against wheat ω5-gliadins (major allergens for this allergy) and against wheat low-molecular weight glutenin subunits (LMW-GS). However, the ability of LMW-GS to trigger an inflammatory response is still unknown. It also remains to be determined if IgE from these patients bind the same epitopes on LMW-GS and ω5-gliadins or if the epitopes are independent. Methods: WDEIA patients were selected and skin prick tests (SPTs) were performed on them using commercial gluten, wheat flour extracts, prolamin fractions and a purified natural LMW-GS P42. The IgE-binding ability of natural and recombinant wheat prolamins was verified by immunoblot experiments. Cross-reactivity between LMW-GS and ω5-gliadins was studied by immunoblot inhibition experiments, using purified natural ω5-gliadin as an inhibitor. Results: Patients developed positive SPTs with natural LMW-GS fractions and/or with the purified LMW-GS P42. Natural and recombinant LMW-GS were highly reactive with patient IgE in immunoblot experiments, as was ω5-gliadin. However, differences in reactivity were evident within the LMW-GS group. Except for one recombinant LMW-GS (P73), IgE cross-reactivity between LMW-GS and natural ω5-gliadin was only partial. Conclusion: LMW-GS are able to promote local inflammation and they share common epitopes with ω5-gliadins. The nature of these epitopes is discussed. LMW-GS also carried specific epitopes, completely independent from the ω5-gliadin epitopes. Thus, LMW-GS behaved partly as independent allergens.

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Common food allergens and their IgE-binding epitopes

Matsuo

Yokooji

Taogoshi

2015

Allergology International

201

135

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Food allergy is an adverse immune response to certain kinds of food. Although any food can cause allergic reactions, chicken egg, cow's milk, wheat, shellfish, fruit, and buckwheat account for 75% of food allergies in Japan. Allergen-specific immunoglobulin E (IgE) antibodies play a pivotal role in the development of food allergy. Recent advances in molecular biological techniques have enabled the efficient analysis of food allergens. As a result, many food allergens have been identified, and their molecular structure and IgE-binding epitopes have also been identified. Studies of allergens have demonstrated that IgE antibodies specific to allergen components and/or the peptide epitopes are good indicators for the identification of patients with food allergy, prediction of clinical severity and development of tolerance. In this review, we summarize our current knowledge regarding the allergens and IgE epitopes in the well-researched allergies to chicken egg, cow's milk, wheat, shrimp, and peanut.

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Recombinant Proteins and Peptides as Tools for Studying IgE Reactivity with Low-Molecular-Weight Glutenin Subunits in Some Wheat Allergies

Cited by 21 publications

References 31 publications

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

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

Low Molecular Weight Glutenins in Wheat-Dependant, Exercise-Induced Anaphylaxis: Allergenicity and Antigenic Relationships with Omega 5-Gliadins

Common food allergens and their IgE-binding epitopes

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