Isolation and Molecular Cloning of a Major Wheat Allergen, Tri a Bd 27K

Kimoto, Masumi; Suzuki, Makiko; Komiyama, Nobuko; Kunimoto, Ayumi; Yamashita, Hiromi; Hiemori, Miki; Takahashi, Kyoko; Tsuji, Hideaki

doi:10.1271/bbb.80485

Cited by 18 publications

(17 citation statements)

References 31 publications

(54 reference statements)

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“…Besides the α‐amylase inhibitors, the 27‐kDa protein with homology to gamma‐interferon‐inducible thiol reductases (30) was the most frequent IgE‐binding protein (16%) in the bakers’ group and was named Tri a 27.0101. The other proteins binding exclusively to bakers’ IgE were αβ‐gliadin named Tri a 21.0101 (10%), peroxiredoxin named Tri a 32.0101 (7.5%), dehydrin named Tri a 35.0101* (5.3%), serpin named Tri a 33.0101 (5%), GAPDH named Tri a 34.0101 (5%) and ω5‐gliadin named Tri a 19 (2.5%).…”

Section: Discussionmentioning

confidence: 99%

Multiple wheat flour allergens and cross-reactive carbohydrate determinants bind IgE in baker’s asthma

Sander

Rozynek

Rihs

et al. 2011

Allergy

119

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Section: Discussionmentioning

confidence: 99%

Multiple wheat flour allergens and cross-reactive carbohydrate determinants bind IgE in baker’s asthma

Sander

Rozynek

Rihs

et al. 2011

Allergy

119

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“…105 Tri a 27 was identified as an allergen that causes wheat protein contact dermatitis and wheat food allergy. 114,134,135 It is considered that the N-linked glycan moieties with fucose residues contained in this allergen are involved in IgE-binding. 136 The highest frequencies of Tri a 27-specific IgE were reported in patients with baker's asthma.…”

Section: Water/salt-soluble Wheat Allergensmentioning

confidence: 99%

Common food allergens and their IgE-binding epitopes

Matsuo

Yokooji

Taogoshi

2015

Allergology International

200

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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“…N-glycosylation was found at an atypical Asn-Leu-Cys consensus sequence (Snegaroff et al 2013). Hiemori et al (2010) and Kimoto et al (2009) confirmed that the major allergens responsible for bakers´ asthma belong to the water/salt-soluble protein fraction of wheat. Some glycoproteins with molecular weight in the 12-16 kDa range from alphaamylase/trypsin inhibitor family are confirmed allergens found in wheat and barley flour (Sanchez-Monge et al 1992;Perrocheau et al 2005).…”

Section: Cereal Glycoproteinsmentioning

confidence: 74%

Cerealn-glycoproteins Enrichment by Lectin Affinity Monolithic Chromatography

Flodrová

Bobáľová

Laštovičková

2016

Cereal Research Communications

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Research of cereal glycoproteins is important for understanding of their functional properties, their role during technological processing of cereals and it can serve as a valuable tool for the detection of cereal allergens. The main intention of this study was the screening of profile of water-soluble glycoproteins present in barley (Hordeum vulgare), wheat durum (Triticum durum) and spelt (Triticum spelta). Lectin monolithic HPLC column was used for rapid and effective enrichment of glycoprotein fractions. Captured glycoproteins were electrophoretically separated and analyzed by MALDI-TOF MS. Presented procedure resulted in identification of a group of N-glycoprotein candidates with affinity to lectin concanavalin A (ConA). Such molecules could have, among others, an allergenic potential. Majority of captured low-molecular-weight glycoproteins belong to alpha amylase/trypsin inhibitors family. However, most of the higher-molecular-weight proteins identified in lectin bound fractions have not been described as glycoproteins yet. Obtained results improved the knowledge about (glyco)protein content in cereal grain. The connection of lectin HPLC-GE-MS was proved as a convenient strategy for identification of cereal glycoproteins. Suggested method is universal and can be applied for various cereals and food-stuffs.

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Isolation and Molecular Cloning of a Major Wheat Allergen, Tri a Bd 27K

Cited by 18 publications

References 31 publications

Multiple wheat flour allergens and cross-reactive carbohydrate determinants bind IgE in baker’s asthma

Multiple wheat flour allergens and cross-reactive carbohydrate determinants bind IgE in baker’s asthma

Common food allergens and their IgE-binding epitopes

Cerealn-glycoproteins Enrichment by Lectin Affinity Monolithic Chromatography

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