Structural Characterization of the 16-kDa Allergen, RA17, in Rice Seeds. Prediction of the Secondary Structure and Identification of Intramolecular Disulfide Bridges

Izumi, Hidehiko; Sugiyama, Minoru; Matsuda, Tsukasa; Nakamura, Ryô

doi:10.1271/bbb.63.2059

Cited by 23 publications

(9 citation statements)

References 21 publications

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“…To date, proteins suspected as being an allergen to rice are 14 to 16 kDa Ory s 12 (profillin A) and 33 kDa or 35 kDa Ory s 1 (beta-expansin)5-7,9). The majority of plant food allergens can be grouped into only 4 protein families.…”

Section: Discussionmentioning

confidence: 99%

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Identification of major rice allergen and their clinical significance in children

Jeon

Yang

et al. 2011

Korean J Pediatr

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PurposeRecently, an increase in the number of patients sensitized to rice allergen with or without clinical symptoms has been reported. This study was designed to determine the major allergens in rice and their clinical significance.MethodsTwenty-four children (15 boys and 9 girls; mean age, 16.3 months) with allergic disease, who were sensitized to rice antigen (by UniCAP) in the Pediatric Allergy Respiratory Center at Soonchunhyang University Hospital, were enrolled in this study. The allergenicity of various types of rice (raw, cooked, and heat-treated, simulated gastric fluid [SGF], and simulated intestinal fluid [SIF]) was investigated using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoglobulin E (IgE) immunoblots. The patients' medical records, including laboratory data and allergy symptoms after ingestion of rice were reviewed.ResultsPatients were sensitized to an average of 13.5 food antigens and their mean total IgE was 6,888.7 kU/L. In SDS-PAGE, more than 16 protein bands were observed in the raw rice, whereas only 14-16 kDa and 31-35 kDa protein bands were observed in cooked rice. The common SDS-PAGE protein bands observed in SGF-, SIF-, and heat-treated rice were 9, 14, and 31 kDa. In a heated-rice IgE immunoblot, protein bands of 9, 14, and 31-33 kDa were found in 27.8%, 38.9%, and 38.9% of all sera, respectively, and in 50%, 50%, and 75%, of ser a from the 4 symptomatic patients, respectively.ConclusionThe 9-, 14-, and 31-kDa protein bands appeared to be the major allergens responsible for rice allergy symptoms.

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Section: Discussionmentioning

confidence: 99%

“…One study reported that globulin in the embryonic bud of rice has strong allergenicity. Another study reported that albumin with protein bands of 14-16 kDa is the major allergen of rice5,6). There are some reports about the protein bands of 26, 33, 56 kDa as the major IgE-binding components in rice7-10).…”

Section: Introductionmentioning

confidence: 98%

Identification of major rice allergen and their clinical significance in children

Jeon

Yang

et al. 2011

Korean J Pediatr

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“…Some examples of sequence comparison and analysis in the study of allergens include molecular characterization of an allergen group from dust mites (36), characterization of a superfamily of proteins containing the allergenic lipid transfer proteins (37), structural characterization of a rice allergen (38), cross-reactivity studies of allergens (27,39), analysis of mutations of pollen allergens (23), study of structural and molecular basis of allergenicity (25), and identification of characteristic motifs in cat (40) or cockroach (24) allergens.…”

Section: Common Bioinformatic Toolsmentioning

confidence: 99%

Computational tools for the study of allergens

Brusic

Petrovsky

Gendel

et al. 2003

Allergy

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Allergy is a major cause of morbidity worldwide. The number of characterized allergens and related information is increasing rapidly creating demands for advanced information storage, retrieval and analysis. Bioinformatics provides useful tools for analysing allergens and these are complementary to traditional laboratory techniques for the study of allergens. Specific applications include structural analysis of allergens, identification of B‐ and T‐cell epitopes, assessment of allergenicity and cross‐reactivity, and genome analysis. In this paper, the most important bioinformatic tools and methods with relevance to the study of allergy have been reviewed.

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“…All these observations suggest that intramolecular disulfide bonding contributes positively to allergenicity. However, there has been little comprehensive analysis of cereal proteins from the standpoint of disulfide bonding (Izumi et al 1999).…”

Section: Identification Of Disulfide Proteins In the Salt Soluble Framentioning

confidence: 99%

Identification of Disulfide Proteins in the Salt Soluble Fraction of Rice (Oryza sativa) Seed

Yano

Kuroda

2003

Cereal Chem

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Evidence has been accumulating to suggest that disulfide bonding is one of the key causes of allergenicity. Recently we developed the “disulfide proteome”, a technique for the comprehensive analysis of disulfide bonding of proteins. We applied this new technique to the rice seed's salt‐soluble fraction, which has long been known to be allergenic. Most proteins in the fraction, including α‐amylase/trypsin inhibsitor, α‐ globulin, and glutelin fragments, have formed intramolecular disulfide bonds. Also, unknown proteins, including one sharing similarities with known allergens, had disulfide bonds, from which we can infer possible allergenicity. This is a preliminary study to screen allergens from the basis of disulfide bonding.

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Structural Characterization of the 16-kDa Allergen, RA17, in Rice Seeds. Prediction of the Secondary Structure and Identification of Intramolecular Disulfide Bridges

Cited by 23 publications

References 21 publications

Identification of major rice allergen and their clinical significance in children

Identification of major rice allergen and their clinical significance in children

Computational tools for the study of allergens

Identification of Disulfide Proteins in the Salt Soluble Fraction of Rice (Oryza sativa) Seed

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