Identification of the Soybean Allergenic Protein,<i>Gly m</i>Bd 30K, with the Soybean Seed 34-kDa Oil-body-associated Protein

Ogawa, Tadashi; Tsuji, Hideaki; Bando, Noriko; Kitamura, Kazuya; Zhu, Yuelin; Hirano, Hisashi; Nishikawa, Kiyoshi

doi:10.1271/bbb.57.1030

Cited by 187 publications

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“…A 30-kD allergen has been described as a protein strongly recognized by the IgE antibodies in sera from soybean-sensitive patients. However, it was isolated from the 7S globulin fraction [16].…”

Section: Discussionmentioning

confidence: 99%

“…The 7S complex is generally a trimer with MW 150-200 kD, whereas 11S is a hexamer with MW 300-400 kD [14]. In the 7S fraction, or b-conglycinin, several IgE-binding proteins have been identified and some of them have been purified and characterized: Gly m Bd 28K, Gly m Bd 30K, Gly m Bd 60K [15,16]. Sequence homology has been reported between these allergens and the thiol proteinase family [17], and with the 49 Detection and identification of a soy protein component that cross-reacts with caseins from cow's milk allergen Der p1.…”

Section: Introductionmentioning

confidence: 99%

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Detection and identification of a soy protein component that cross-reacts with caseins from cow's milk

Rozenfeld

Docena

Añón

et al. 2002

Clinical and Experimental Immunology

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Food allergy is becoming a medical, economical and social problem. Soybean, together with milk, peanuts and eggs, are the major allergenic foods. This pathology affects the infant population, when the gut barrier is immature and the immune system is still refining its ability to tolerate food proteins. In our country, cow's milk allergy (CMA) constitutes the main food allergy in infancy, but soy allergy has become exacerbated because of the increased utilization of soy-based formulas as cow's milk (CM) substitutes and the inclusion of soy-proteins in many processed foods. Once a food allergy is diagnosed, the only proven therapy is the strict elimination of the offending allergens from the diet. Available substitutes for CM include milks from different mammalian animals, soy-based formulas, hydrolysed cow's milk proteins (CMP) and amino acid-based formulas. Furthermore, there is evidence that soy proteins may trigger allergic reactions in CMA patients, as assessed by a double-blind placebo controlled food challenge (DBPCFC) [1].Milk contains more than 50 proteins and the major ones are implicated in a number of immunologically mediated reactions [2]. Caseins and b-lactoglobulin (b-Lg) have been described as the main antigenic and allergenic components for human beings [3,4], although immunoglobulins, a-lactalbumin (a-La), and bovine serum albumin (BSA) were also found to be reactive with different isotypes of human antibodies [5,6]. Several immunoreactive epitopes have been identified in caseins [7,. Most of the epitopes present in the casein molecules are sequential since the high number of proline and hydrophobic residues (45%) in these proteins determine an undefined secondary and tertiary structure [10]. Besides, caseins tend to aggregate as a result of hydrophobic interactions to give quaternary structures [11], and this may create conformational epitopes buried in the hydrophobic interior of the micelle [7]. These epitopes are only exposed and accessible to the immune system after denaturation of the complex by digestion.A number of soy proteins that bind antibodies, especially IgE, have been identified [12,13]. The main fractions of storage globulins from seed proteins are the complexes 7S or b-conglycinin, and 11S or glycinin. The 7S complex is generally a trimer with MW 150-200 kD, whereas 11S is a hexamer with MW 300-400 kD [14]. In the 7S fraction, or b-conglycinin, several IgE-binding proteins have been identified and some of them have been purified and characterized: Gly m Bd 28K, Gly m Bd 30K, Gly m Bd 60K [15,16]. Sequence homology has been reported between these allergens and the thiol proteinase family SUMMARYSoy-based formulas are the most employed cow's milk substitutes in the treatment of cow's milk allergy in our country. Since adverse reactions have been reported in allergic patients as a consequence of exposure to soy proteins, we have investigated the possible cross-reactivity between components from soybean and cow's milk. A cow's milk specific polyclonal antiserum and casein specific m...

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Detection and identification of a soy protein component that cross-reacts with caseins from cow's milk

Rozenfeld

Docena

Añón

et al. 2002

Clinical and Experimental Immunology

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“…Soy protein is a well-known allergenic protein, and the 34 kDa protein is a well identified allergenic protein in soy protein (Ogawa et al , 1993). Most patients who can not take soy protein are sensitive to 34 kDa protein.…”

Section: Masking Of Allergen Structure Of Proteinsmentioning

confidence: 99%

Industrial Applications of Maillard-Type Protein-Polysaccharide Conjugates.

Kato¹

2002

FSTR

233

139

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This review summarizes the properties of Maillard-type protein-polysaccharide conjugates through naturally occurring reaction in a dry state from the viewpoint of the development of new industrial proteins. Maillard-type protein-polysaccharide conjugates showed excellent emulsifying properties superior to conventional commercial emulsifiers, heat stability, and antimicrobial activity. Therefore, the conjugates can be useful for industrial applications as natural emulsifiers, antimicrobial agents devoid of toxicity. The possibility has also been proposed that conjugation of the allergen protein with polysaccharides may be effective to reduce the allergenicity. The molecular mechanism of the improvement of functional properties of proteins by attachment with polysaccharide was elucidated using the genetically glycosylated lysozyme constructed in the yeast expression system. The polymannosylation of lysozyme was effective in improving these functional properties, while oligomannosylation was not. Although single polyglycosylation of lysozyme was adequate to improve the functional properties, double polyglycosylation was even better.

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“…In this study, we used the following primary antibodies against the major soybean allergens listed in Table 2: anti-7S globulin (rabbit polyclonal antibody) (12), anti-Gly m Bd 30K (mouse monoclonal antibody) (13), anti-Gly m Bd 28K (mouse monoclonal antibody) (14), anti-Gly m 4 and anti-Gly m 3 (rabbit polyclonal antibodies), and anti-soybean trypsin inhibitor (rabbit polyclonal antibody; Chemicon, Temecula, CA). All antibodies used in this study except for antisoybean trypsin inhibitor were prepared by us or other researchers.…”

Section: Methodsmentioning

confidence: 99%

Hypoallergenicity of Various Miso Pastes Manufactured in Japan

Moriyama

Yano

Suemori

et al. 2013

J Nutr Sci Vitaminol

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Summary Miso paste (miso), a fermented soybean food, is popular in Japan and other Asian countries. However, the soybean is known to induce an allergenic response in some individuals. In the present study, we evaluated the allergenicity of various kinds of miso available in Japan. Total proteins were extracted from Amakuti-kome miso, Karakuti-kome miso, Mugi-miso and Mame-miso, and the protein profiles were analyzed. The major protein bands detected in the intact soybean extract were not present in any of the miso samples, which instead showed various low molecular weight protein bands of approximately 10-25 kDa. The existence levels of six major soybean allergens were determined by Western blotting using specific antibodies. We found that the allergen levels varied among miso and allergen types; however, allergen levels were consistently lower in miso than in the soybean extract. We obtained similar results for IgE-ELISA experiments using serum IgE from soybean allergy patients. Taken together, these results indicate that compared to soybean extract, various types of miso contain small quantities of intact soybean allergens. Additionally, several lines of evidence indicated that the allergen levels were exceptionally low in the dark-colored Karakuti-kome miso and Mame-miso, which are produced with relatively long fermentation periods, suggesting that the duration of fermentation might be a key factor in the hypoallergenicity of miso.

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Identification of the Soybean Allergenic Protein,Gly mBd 30K, with the Soybean Seed 34-kDa Oil-body-associated Protein

Cited by 187 publications

References 0 publications

Detection and identification of a soy protein component that cross-reacts with caseins from cow's milk

Detection and identification of a soy protein component that cross-reacts with caseins from cow's milk

Industrial Applications of Maillard-Type Protein-Polysaccharide Conjugates.

Hypoallergenicity of Various Miso Pastes Manufactured in Japan

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