Digestibility of peanut and hazelnut allergens investigated by a simple in vitro procedure

Vieths, Stefan; Reindl, Jürgen; Müller, Ursula; Hoffmann, Andreas; Haustein, Dieter

doi:10.1007/s002170050513

Cited by 79 publications

(80 citation statements)

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“…Gastric in vitro digestion of wheat extracts and rTri a 36 was performed as described (29). For the duodenal digestion, Pankreoflat commercial enzyme tablets (Solvay Pharma, Hannover, Germany) were used.…”

Section: In Vitro Digestion Assaysmentioning

confidence: 99%

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Baar

Pahr

Constantin

et al. 2012

The Journal of Immunology

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Wheat is an essential element in our nutrition but one of the most important food allergen sources. Wheat allergic patients often suffer from severe gastrointestinal and systemic allergic reactions after wheat ingestion. In this study, we report the molecular and immunological characterization of a new major wheat food allergen, Tri a 36. The cDNA coding for a C-terminal fragment of Tri a 36 was isolated by screening a wheat seed cDNA expression library with serum IgE from wheat food-allergic patients. Tri a 36 is a 369-aa protein with a hydrophobic 25-aa N-terminal leader peptide. According to sequence comparison it belongs to the low m.w. glutenin subunits, which can be found in a variety of cereals. The mature allergen contains an N-terminal domain, a repetitive domain that is rich in glutamine and proline residues, and three C-terminal domains with eight cysteine residues contributing to intra- and intermolecular disulfide bonds. Recombinant Tri a 36 was expressed in Escherichia coli and purified as soluble protein. It reacted with IgE Abs of ∼80% of wheat food-allergic patients, showed IgE cross-reactivity with related allergens in rye, barley, oat, spelt, and rice, and induced specific and dose-dependent basophil activation. Even after extensive in vitro gastric and duodenal digestion, Tri a 36 released distinct IgE-reactive fragments and was highly resistant against boiling. Thus, recombinant Tri a 36 is a major wheat food allergen that can be used for the molecular diagnosis of, and for the development of specific immunotherapy strategies against, wheat food allergy.

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Section: In Vitro Digestion Assaysmentioning

confidence: 99%

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Baar

Pahr

Constantin

et al. 2012

The Journal of Immunology

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“…Simulated gastric fluid (SGF) was prepared with a pharmaceutical enzyme tablet (Enzynorm ® forte, Pharmaselect Handels GmbH, Vienna, Austria) as previously described [14] with slight modifications: one tablet was dissolved in 100 μL 0.9% sterile sodium chloride at pH 2.0 or pH 5.0. For digestion, 500 μL of SGF was incubated with 500 μg OVA.…”

Section: The Model Allergen Ovalbuminmentioning

confidence: 99%

Dose-dependent food allergy induction against ovalbumin under acid-suppression: A murine food allergy model

et al. 2008

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Background-Animal models are essential for analyzing the allergenic potential of food proteins and for investigating mechanisms underlying food allergy. Based on previous studies revealing acid-suppression medication as risk factor for food allergy induction, we aimed to establish a mouse model mimicking the natural route of sensitization in patients.Methods-The effect of acid-suppressing medication on murine gastric pH was assessed by intragastric pH measurements after two injections of a proton pump inhibitor (PPI). To investigate dose-dependency, mice were fed different concentrations of ovalbumin (OVA; 0.2, 0.5, 1.0, 2.5 or 5.0 mg) either with or without anti-ulcer medication. Additionally, different routes of exposure (i.p. vs. oral) were compared in a second immunization experiment. Sera were screened for OVAspecific antibody titers (IgG1, IgG2a and IgE) in ELISA and RBL assay. Clinical reactivity was evaluated by measuring rectal temperature after oral challenge and by type I skin tests.Results-Two intravenous injections of PPI significantly elevated the gastric pH from 2.97 to 5.3. Only oral immunization with 0.2 mg OVA under anti-acid medication rendered elevated IgG1, IgG2a and IgE titers compared to all other concentrations. Protein feeding alone altered antibody titers only marginally. Even though also i.p. immunizations induced high levels of specific IgE, only oral immunizations under anti-acids induced anaphylactic reactions evidenced by a significant decrease of body temperature.Conclusion-Only low-dosage ovalbumin feedings under anti-acid medication resulted in IgE mediated food allergy. Based on this knowledge we have established a suitable food allergy model for further investigations of food adverse reactions.

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“…First, a gastric digestion according to Astwood et al [32] and, second, a duodenal digestion according to Vieths et al [33] with modifications of Astwood et al was performed. Gastric and duodenal conditions were simulated using commercial enzyme tablets which are used to substitute individuals with reduced pepsin production or pancreas function.…”

Section: In Vitro Digestionmentioning

confidence: 99%

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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Digestibility of peanut and hazelnut allergens investigated by a simple in vitro procedure

Cited by 79 publications

References 0 publications

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Dose-dependent food allergy induction against ovalbumin under acid-suppression: A murine food allergy model

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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