Food‐dependent exercise‐induced anaphylaxis: a report of two cases and determination of wheat‐γ‐gliadin as the presumptive allergen

Morita, Eishin; Yamamura, Y; Mihara, Shoji; Kameyoshi, Yoshikazu; Yamamoto, Shoso

doi:10.1046/j.1365-2133.2000.03844.x

Cited by 43 publications

(30 citation statements)

References 15 publications

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“…Proteins in the water/ salt-soluble fraction, such as ␣-amylase inhibitor, peroxidase, glycerinaldehyde-3-phosphate dehydrogenase, serpin, and triosephosphate isomerase, have been identified to be major allergens in patients with baker's asthma (27)(28)(29). ␣-Gliadin, ␥-gliadin, and -5 gliadin in water/salt-insoluble fraction have been identified as allergens in WDEIA (17,30,31). However, in patients with classical wheat allergy, the allergens responsible for symptoms have not been defined because serum IgE reacted to both water/saltsoluble and -insoluble proteins (32-36).…”

Section: Discussionmentioning

confidence: 99%

Specific IgE Determination to Epitope Peptides of ω-5 Gliadin and High Molecular Weight Glutenin Subunit Is a Useful Tool for Diagnosis of Wheat-Dependent Exercise-Induced Anaphylaxis

Matsuo

Kohno

Niihara

et al. 2005

The Journal of Immunology

165

126

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Wheat ω-5 gliadin and a high m.w. glutenin subunit (HMW-glutenin) have been reported as major allergens in wheat-dependent exercise-induced anaphylaxis. A simultaneous detection of specific IgE to epitope sequences of both proteins is considered to be a reliable method for diagnosis of wheat-dependent exercise-induced anaphylaxis. However, the IgE-binding epitope of HMW-glutenin remains unknown. The aim of this study was to determine the IgE-binding epitopes of HMW-glutenin to establish a useful system of identifying patients with wheat-dependent exercise-induced anaphylaxis. For determination of IgE-binding epitopes of HMW-glutenin overlapping peptides were synthesized and reactivities of IgE Abs in the sera of patients to those peptides were analyzed. Three IgE-binding epitopes, QQPGQ, QQPGQGQQ, and QQSGQGQ, were identified within primary sequence of HMW-glutenin. Epitope peptides, which include IgE-binding sequences of ω-5 gliadin and a HMW-glutenin, were synthesized and peptide-specific IgE Abs were measured by CAP-System fluorescent enzyme immunoassay. Twenty-nine of 30 patients with wheat-dependent exercise-induced anaphylaxis had specific IgE Abs to these epitope peptides. None of the 25 sera from healthy subjects reacted to both epitope peptides. Twenty-five patients with atopic dermatitis who had specific IgE to wheat and/or gluten had very low or nonexistent levels of epitope peptide-specific IgE Abs. These results indicated that measurement of IgE levels specific to epitope peptides of ω-5 gliadin and HMW-glutenin is useful as an in vitro diagnostic method for the assessment of patients with wheat-dependent exercise-induced anaphylaxis.

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Section: Discussionmentioning

confidence: 99%

Specific IgE Determination to Epitope Peptides of ω-5 Gliadin and High Molecular Weight Glutenin Subunit Is a Useful Tool for Diagnosis of Wheat-Dependent Exercise-Induced Anaphylaxis

Matsuo

Kohno

Niihara

et al. 2005

The Journal of Immunology

165

126

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“…Water insoluble gliadins have been implicated as prominent factors [10,11]. In a study from Finland, 18 patients with wheat-triggered FT-EIA were tested for immunoglobulin E (IgE) antibodies by immunoblotting of wheat proteins in the presence of the patient's serum.…”

Section: Food-triggered Exercise-induced Anaphylaxismentioning

confidence: 99%

Exercise-induced anaphylaxis

Castells

Horan

Sheffer

2003

Curr Allergy Asthma Rep

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Exercise-induced anaphylaxis has been recognized with increasing frequency since its original description in 1980. Recent studies suggest food-induced reactions may occur frequently in this syndrome, which is a mast cell-dependent phenomenon. In this article, the clinical manifestations of exercise-induced anaphylaxis are reviewed, and food-related factors contributing to the disorder are considered.

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“…All subjects had IgE antibodies against a 65 kDa omega-5 gliadin (Tri a 19) which appeared to be a major allergen for this form of wheat allergy. A 65 kDa gliadin was also described as an allergen by two other authors, in connection with exercise-induced anaphylaxis and dermatitis herpetiformis, respectively [18,19]. Several major wheat allergens were described by different investigators who preferentially analyzed one of the three forms of wheat allergy: food allergy [20 -22], wheat-dependent, exercise-induced anaphylaxis [16], baker's asthma [23,24], or atopic dermatitis [25,26].…”

Section: Introductionmentioning

confidence: 97%

Immunoglobulin E‐reactivity of wheat‐allergic subjects (baker's asthma, food allergy, wheat‐dependent, exercise‐induced anaphylaxis) to wheat protein fractions with different solubility and digestibility

Mittag

Niggemann

Sander

et al. 2004

Molecular Nutrition Food Res

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Baker's asthma, food allergy to wheat, and wheat-dependent, exercise-induced anaphylaxis (WDEIA) are different clinical forms of wheat allergy. We investigated the correlation of solubility and digestion stability of wheat allergens with the IgE-reactivity patterns of different patient groups. Three wheat protein fractions were extracted according to their solubility: salt-soluble albumins and globulins, ethanol-soluble gliadins, and glutenins soluble only after treatment with detergents and reducing reagents. Sera from subjects with history of each variant of wheat allergy were characterized by CAP FEIA and immunoblotting. There was a high degree of heterogeneity of recognized allergens between the different subject groups as well as within these groups. However, subjects with WDEIA showed similar immunoglobulin E (IgE)-reactivity patterns to gliadins and especially to a 65 kDa protein. Subjects with baker's asthma as well as the food-allergic subjects had the most intense IgE-reactivity to the albumin/globulin fraction. The latter group additionally showed IgE-reactivity to the other fractions. Divergent results of immunoblotting and CAP-FEIA demonstrated that the detection of wheat-specific IgE highly depends on the applied method, thus the diagnostic tool must be carefully chosen. Most wheat allergens were rapidly digested as analyzed by determination of IgE-reactivity on immunoblots to wheat extracts after simulation of gastric and duodenal digestion. However, ethanol-soluble gliadins were stable to gastric enzymes and exhibit low solubility in gastric and duodenal fluids. Therefore, they are likely to be important in food allergy to wheat.

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Food‐dependent exercise‐induced anaphylaxis: a report of two cases and determination of wheat‐γ‐gliadin as the presumptive allergen

Cited by 43 publications

References 15 publications

Specific IgE Determination to Epitope Peptides of ω-5 Gliadin and High Molecular Weight Glutenin Subunit Is a Useful Tool for Diagnosis of Wheat-Dependent Exercise-Induced Anaphylaxis

Specific IgE Determination to Epitope Peptides of ω-5 Gliadin and High Molecular Weight Glutenin Subunit Is a Useful Tool for Diagnosis of Wheat-Dependent Exercise-Induced Anaphylaxis

Exercise-induced anaphylaxis

Immunoglobulin E‐reactivity of wheat‐allergic subjects (baker's asthma, food allergy, wheat‐dependent, exercise‐induced anaphylaxis) to wheat protein fractions with different solubility and digestibility

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