Identification of Alpha-Amylase Inhibitor as a Major Allergen of Wheat Flour

Franken, Jan; Stephan, Udo W.; Meyer, Helmut E.; König, W.

doi:10.1159/000236726

Cited by 59 publications

(35 citation statements)

References 8 publications

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“…In addition, it was predicted that the 0.19 inhibitor might become a potent allergen if it coexisted with the 0.53 inhibitor [5]. Here we demonstrate for the first time that the 0.19 and 0.53 inhibitors may naturally exist as heterodimers, an aggregation state that might be correlated to a higher risk for human health.…”

Section: -D Analysis Of Dimeric Inhibitors From T Aestivum and Demomentioning

confidence: 58%

“…It is noteworthy that dimeric a-AIs, and in particular the 0.19 [5,6], have been described as major allergens of baker's asthma. In addition, it was predicted that the 0.19 inhibitor might become a potent allergen if it coexisted with the 0.53 inhibitor [5].…”

Section: -D Analysis Of Dimeric Inhibitors From T Aestivum and Demomentioning

confidence: 99%

“…However, certain members of the family are active on human amylases, and hence are bioactive on human gastrointestinal tract. Moreover, wheat inhibitors are considered as major crop allergens, involved in pathologies like baker's asthma [5][6][7]. Their bioactive potential is furthermore investigated as a pharmacologic tool to treat diabetes, obesity and hyperlipemia [8].…”

Section: Introductionmentioning

confidence: 99%

“…Within the dimeric group are a-AIs specific for human a-amylase and with allergenic potential, and indeed members from this group are considered by some authors the major allergen in baker's asthma, an occupational hypersensitivity disease with serious consequences [5,6].…”

Section: Introductionmentioning

confidence: 99%

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Full‐fledged proteomic analysis of bioactive wheat amylase inhibitors by a 3‐D analytical technique: Identification of new heterodimeric aggregation states

et al. 2007

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Full-fledged proteomic analysis of bioactive wheat amylase inhibitors by a 3-D analytical technique: Identification of new heterodimeric aggregation statesWheat proteinaceous a-amylase inhibitors (a-AIs) are increasingly investigated for their agronomical role as natural defence molecules of plants against the attack of insects and pests, but also for their effects on human health. The wheat genomes code for several bioactive a-AIs that share sequence homology, but differ in their specificity against a-amylases from different species and for their aggregation states. Wheat a-AIs are traditionally classified as belonging to the three classes of tetrameric, homodimeric and monomeric forms, each class being constituted by a number of polypeptides that display different electrophoretic mobilities. Here we describe a proteomic approach for the identification of bioactive a-AIs from wheat and, in particular, a 3-D technique that allows to best identify and characterize the dimeric fraction. The technique takes advantage of the thermal resistance of a-AIs (resistant to T . 707C) and consists in the separation of protein mixtures by 2-D polyacrylamide/starch electrophoresis under nondissociating PAGE (ND-PAGE, first dimension) and dissociating (urea-PAGE or U-PAGE second dimension) conditions, followed by in-gel spontaneous reaggregation of protein complexes and identification of the a-amylase inhibitory activity (antizymogram, third dimension) using enzymes from human salivary glands and from the larvae of Tenebrio molitor coleopter (yellow mealworm). Dimeric a-AIs from Triticum aestivum (bread wheat) were observed to exist as heterodimers. The formation of heterodimeric complexes was also confirmed by in vitro reaggregation assays carried out on RP-HPLC purified wheat dimeric a-AIs, and their bioactivity assayed by antizymogram analysis. The present 3-D analytical technique can be exploited for fast, full-fledged identification and characterization of wheat a-AIs.

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Section: -D Analysis Of Dimeric Inhibitors From T Aestivum and Demomentioning

confidence: 58%

Section: -D Analysis Of Dimeric Inhibitors From T Aestivum and Demomentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Full‐fledged proteomic analysis of bioactive wheat amylase inhibitors by a 3‐D analytical technique: Identification of new heterodimeric aggregation states

et al. 2007

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“…Human wheat allergic subjects can be sensitive to a number of proteins present in the alcohol-soluble, acid-soluble, and salt-soluble protein fractions from wheat [1,2,3,8,19,20]. Although mouse models for wheat allergy have been developed for gluten proteins (gliadins), a mouse model for SSWPs - another major group of wheat allergens in both the USA and Europe - was not available.…”

Section: Discussionmentioning

confidence: 99%

A Mouse Model of Anaphylaxis and Atopic Dermatitis to Salt-Soluble Wheat Protein Extract

Jin

Ebaugh

Martens

et al. 2017

Int Arch Allergy Immunol

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Background: Wheat allergy and other immune-mediated disorders triggered by wheat proteins are growing at an alarming rate for reasons not well understood. A mouse model to study hypersensitivity responses to salt-soluble wheat protein (SSWP) extract is currently unavailable. Here we tested the hypothesis that SSWP extract from wheat will induce sensitization as well as allergic disease in mice. Methods: Female BALB/cJ mice were weaned onto a plant protein-free diet. The mice were injected a total of 4 times with an SSWP (0.01 mg/mouse) fraction extracted from durum wheat along with alum as an adjuvant. Blood was collected biweekly and SSWP-specific IgE (SIgE) and total IgE (TIgE) levels were measured using ELISA. Systemic anaphylaxis upon intraperitoneal injection with SSWP was quantified by hypothermia shock response (HSR). Mucosal mast cell degranulation was measured by the elevation of mMCP-1 in the blood. The mice were monitored for dermatitis. Skin tissues were used in histopathology and for measuring cytokine/chemokine/adhesion molecule levels using a protein microarray system. Results: Injection with SSWP resulted in time-dependent SIgE antibody responses associated with the elevation of TIgE concentration. Challenge with SSWP elicited severe HSR that correlated with a significant elevation of plasma mMCP-1 levels. Sensitized mice developed facial dermatitis associated with mast cell degranulation. Lesions expressed significant elevation of Th2/Th17/Th1 cytokines and chemokines and E-selectin adhesion molecule. Conclusion: Here we report a mouse model of anaphylaxis and atopic dermatitis to SSWP extract that may be used for further basic and applied research on wheat allergy.

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Occupational respiratory allergy in bakery workers: A review of the literature

1998

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Baker's asthma has long been recognized as a serious disease among workers in the bakery industry and the number of cases with baker's asthma is steadily increasing. This paper presents a review of the available literature on baker's allergy with a special focus on the allergens involved, the epidemiologic research and issues on exposure assessment, evidence of exposure‐response‐relationships, and possible prevention strategies. A large number of potential allergens have been identified and are described here. At present little is known about the incidence of baker's allergy. On the other hand, a large number of cross‐sectional studies have been performed, showing that sensitization and work‐related symptoms are common among bakery workers. Only atopy and exposure level have consistently been reported as determinants of this occupational disease. Age, gender, and smoking habits do not seem to be associated with sensitization or work‐related respiratory symptoms. Recently, immunochemical methods have been developed to measure specific allergens in the bakery industry, which have been used to unravel the role of allergen exposure in the development of baker's asthma. Clear exposure‐response‐relationships have been found. The implications of these recent findings for prevention strategies and standard setting are discussed. Am. J. Ind. Med. 34:529–546, 1998. © 1998 Wiley‐Liss, Inc.

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Identification of Alpha-Amylase Inhibitor as a Major Allergen of Wheat Flour

Cited by 59 publications

References 8 publications

Full‐fledged proteomic analysis of bioactive wheat amylase inhibitors by a 3‐D analytical technique: Identification of new heterodimeric aggregation states

Full‐fledged proteomic analysis of bioactive wheat amylase inhibitors by a 3‐D analytical technique: Identification of new heterodimeric aggregation states

A Mouse Model of Anaphylaxis and Atopic Dermatitis to Salt-Soluble Wheat Protein Extract

Occupational respiratory allergy in bakery workers: A review of the literature

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