Update on wheat hypersensitivity

Palosuo, Kati

doi:10.1097/00130832-200306000-00009

Cited by 116 publications

(85 citation statements)

References 45 publications

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“…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). As just described, it is considered that causative allergens are variable among the clinical forms (37,38). Recent studies have shown that -5 gliadin is a good candidate as a diagnostic tool for not only WDEIA but also immediate allergy to wheat (39 -41).…”

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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“…The main symptom of food allergy to wheat in children is atopic eczema/ dermatitis syndrome (AEDS), 7,8) whereas in adults, the most frequent and severe symptom is wheat-dependent exercise-induced anaphylaxis (WDEIA). 7,9,10) Gliadins and glutenins, the major proteins of wheat flour, are involved in the development of food allergy to wheat.…”

Section: Improvement Of Digestibility Reduction In Allergenicity Anmentioning

confidence: 99%

Improvement of Digestibility, Reduction in Allergenicity, and Induction of Oral Tolerance of Wheat Gliadin by Deamidation

Kumagai

Suda

Sakurai

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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“…10,11 . Food allergy is generally caused by a cross-linking of allergens and human immunoglobulin E (IgE), and degranulation of mast cells 2,6 .…”

Section: Introductionmentioning

confidence: 99%

“…IgE recognizes linear 5～10 amino acid sequences of allergen proteins, which are termed epitopes. Among many wheat allergen proteins, gliadins and glutenins have been well studied [10][11][12] . Tanabe et al identified a glutenin epitope (QQQPP) 15 and gliadin epitopes (PQQPF and QQPFP) 16 for atopic dermatitis.…”

Section: Introductionmentioning

confidence: 99%

Degradation of Wheat Epitope Peptides for Atopic Dermatitis and Exercise-Induced Anaphylaxis by Microbial Proteases

Oita

2012

JARQ

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Epitope peptides of wheat gliadins and glutenins for atopic dermatitis, PQQPF and QQQPP, were degraded by the microbial proteases of Streptomyces griseus and Aspergillus oryzae. The proteases of Bacillus licheniformis and Bacillus amyloloiquefasiens degraded wheat gliadins and glutenins, but had little or no effect on the epitopes. A 16-mer peptide of CSQQQQPPFSQQQPPF, which incorporated this glutenin epitope twice, was also hydrolyzed by these proteases, and no peptide containing QQQPP was shown after the reaction with S. griseus protease. The proteases of S. griseus and A. oryzae also degraded epitope peptides of wheat gliadins and glutenins for exercise-induced anaphylaxis, QQIPQQQ, QQFPQQQ and QQPGQ.

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Update on wheat hypersensitivity

Cited by 116 publications

References 45 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

Improvement of Digestibility, Reduction in Allergenicity, and Induction of Oral Tolerance of Wheat Gliadin by Deamidation

Degradation of Wheat Epitope Peptides for Atopic Dermatitis and Exercise-Induced Anaphylaxis by Microbial Proteases

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