Investigation of Multiple Forms of Tri a Bd 27K, a Major Wheat Allergen, by Immunoblotting Analysis

Hiemori, Miki; Yosida, Yukari; Kimoto, Masumi; Yamashita, Hiromi; Takahashi, Kyoko; Takahashi, Kiyoshi; Komiyama, Nobuko; Tsuji, Hideaki

doi:10.1271/bbb.90634

Cited by 9 publications

(11 citation statements)

References 10 publications

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“…3). The much lower digestibility of albumins compared to that of gluten may be attributed to the presence of proteolytic resistant proteins such as peroxidase and α‐amylase inhibitors in water‐soluble proteins 25–27 . Hassan et al 28 .…”

Section: Resultsmentioning

confidence: 99%

“…However, SRW wheat showing a relatively high albumin digestibility had a lower intensity of undigested bands than durum wheat, which showed a relatively low albumin digestibility, indicating that those undigested bands contribute to the low albumin digestion in durum wheat. Water‐soluble proteins (albumins) isolated from wheat flour are reported to contain three major wheat allergens with molecular weights of 17, 27 and 36 kDa 25–27 . Among the wheat classes, large differences in the SDS‐PAGE band densities of proteins with molecular weights of 14–18 kDa, 26–28 kDa and 36 kDa were observed (see Supporting information, Fig.…”

Section: Resultsmentioning

confidence: 99%

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Influences of grain and protein characteristics on in vitro protein digestibility of modern and ancient wheat species

Baik

2021

J Sci Food Agric

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BACKGROUND The resistance of proteins to gastrointestinal digestion contributes to their ability to act as allergens. Near‐complete digestion of protein in wheat products is important with respect to avoiding the potential immunogenic effects of undigested peptides. Five modern US wheat classes (soft red winter, hard winter, hard red spring, club and durum) including 17 wheat varieties, as well as three ancient wheat classes (spelt, emmer and einkorn) including nine wheat varieties, were analyzed for kernel hardness (KH) and flour protein characteristics, in addition to in vitro protein digestibility (IVPD) of cooked flour, flour without albumins and globulins (FWOAG), gluten, albumins, and globulins, aiming to identify the factors influencing the protein digestibility of flour. RESULTS IVPDs of flour, FWOAG, gluten and albumins of wheat varieties ranged from 86.5% to 92.3%, 85.8% to 90.3%, 90.6% to 94.6% and 74.8% to 85.1%, respectively. The IVPD of gluten was significantly higher than the IVPDs of flour and FWOAG, indicating that non‐protein components substantially affect protein digestibility. Significant differences were observed in IVPDs of flour and albumins among eight wheat classes, but not in the IVPDs of FWOAG, gluten and globulins. There were apparent differences in undigested protein bands and intensities of wheat classes with low and high flour IVPDs. KH and albumin proportion exhibited negative and positive relationships, respectively, with flour IVPD. CONCLUSION The results of the present study demonstrate that KH, non‐protein components and albumin proportion have a major influence on protein digestion and need to be considered when developing wheat cultivars with higher protein digestibility.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Influences of grain and protein characteristics on in vitro protein digestibility of modern and ancient wheat species

Baik

2021

J Sci Food Agric

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“…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. 121 Tri a 37 was recently reported as a novel wheat allergen specific for patients with wheat food allergy.…”

Section: Water/salt-soluble Wheat Allergensmentioning

confidence: 98%

Common food allergens and their IgE-binding epitopes

Matsuo

Yokooji

Taogoshi

2015

Allergology International

208

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: 75%

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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Investigation of Multiple Forms of Tri a Bd 27K, a Major Wheat Allergen, by Immunoblotting Analysis

Cited by 9 publications

References 10 publications

Influences of grain and protein characteristics on in vitro protein digestibility of modern and ancient wheat species

Influences of grain and protein characteristics on in vitro protein digestibility of modern and ancient wheat species

Common food allergens and their IgE-binding epitopes

Cerealn-glycoproteins Enrichment by Lectin Affinity Monolithic Chromatography

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