{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1360861291384166272.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.4049/jimmunol.151.10.5354"}},{"identifier":{"@type":"URI","@value":"https://academic.oup.com/jimmunol/article-pdf/151/10/5354/62222786/5354.pdf"}}],"dc:title":[{"@value":"Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes."}],"description":[{"type":"abstract","notation":[{"@value":"<jats:title>Abstract</jats:title>\n               <jats:p>The major heat-stable shrimp allergen (designated as Sa-II), capable of provoking IgE-mediated immediate type hypersensitivity reactions after the ingestion of cooked shrimp, has been shown to be a 34-kDa heat-stable protein containing 300 amino acid residues. Here, we report that a comparison of amino acid sequences of different peptides generated by proteolysis of Sa-II revealed an 86% homology with tropomyosin from Drosophila melanogaster, suggesting that Sa-II could be the shrimp muscle protein tropomyosin. To establish that Sa-II is indeed tropomyosin, the latter was isolated from uncooked shrimp (Penaeus indicus) and its physicochemical and immunochemical properties were compared with those of Sa-II. Both tropomyosin and Sa-II had the same molecular mass and focused in the isoelectric pH range of 4.8 to 5.4. In the presence of 6 M urea, the mobility of both Sa-II and shrimp tropomyosin shifted to give an apparent molecular mass of 50 kDa, which is a characteristic property of tropomyosins. Shrimp tropomyosin bound to specific IgE antibodies in the sera of shrimp-sensitive patients as assessed by competitive ELISA inhibition and Western blot analysis. Tryptic maps of both Sa-II and tropomyosin as obtained by reverse phase HPLC were superimposable. Dot-blot and competitive ELISA inhibition using sera of shrimp-sensitive patients revealed that antigenic as well as allergenic activities were associated with two peptide fractions. These IgE-binding tryptic peptides were purified and sequenced. Mouse anti-anti-idiotypic antibodies raised against Sa-II specific human idiotypic antibodies recognized not only tropomyosin but also the two allergenic peptides, thus suggesting that these peptides represent the major IgE binding epitopes of tropomyosin. A comparison of the amino acid sequence of shrimp tropomyosin in the region of IgE binding epitopes (residues 50-66 and 153-161) with the corresponding regions of tropomyosins from different vertebrates confirmed lack of allergenic cross-reactivity between tropomyosins from phylogenetically distinct species.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380016864050254720","@type":"Researcher","foaf:name":[{"@value":"K N Shanti"}],"jpcoar:affiliationName":[{"@value":"Laboratory of Immunology and Allergic Diseases, Department of Biochemistry, Indian Institute of Science , Bangalore 560012 ,"}]},{"@id":"https://cir.nii.ac.jp/crid/1380861291384166272","@type":"Researcher","foaf:name":[{"@value":"B M Martin"}],"jpcoar:affiliationName":[{"@value":"Clinical Neurosciences Branch, National Institute of Mental Health, National Institutes of Health , Bethesda, MD 20892"}]},{"@id":"https://cir.nii.ac.jp/crid/1380861291384166273","@type":"Researcher","foaf:name":[{"@value":"S Nagpal"}],"jpcoar:affiliationName":[{"@value":"Laboratory of Immunology and Allergic Diseases, Department of Biochemistry, Indian Institute of Science , Bangalore 560012 ,"}]},{"@id":"https://cir.nii.ac.jp/crid/1380861291384166276","@type":"Researcher","foaf:name":[{"@value":"D D Metcalfe"}],"jpcoar:affiliationName":[{"@value":"Mast Cell Physiology Section, Laboratory of Clinical Investigation, National Institute of Allergy and Infectious Diseases, National Institutes of Health , Bethesda, MD 20892"}]},{"@id":"https://cir.nii.ac.jp/crid/1380303972392116864","@type":"Researcher","foaf:name":[{"@value":"P V S Rao"}],"jpcoar:affiliationName":[{"@value":"Laboratory of Immunology and Allergic Diseases, Department of Biochemistry, Indian Institute of Science , Bangalore 560012 ,"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00221767"},{"@type":"EISSN","@value":"15506606"},{"@type":"PISSN","@value":"http://id.crossref.org/issn/00221767"}],"prism:publicationName":[{"@value":"The Journal of Immunology"}],"dc:publisher":[{"@value":"Oxford University Press (OUP)"}],"prism:publicationDate":"1993-11","prism:volume":"151","prism:number":"10","prism:startingPage":"5354","prism:endingPage":"5363"},"reviewed":"false","dc:rights":["https://academic.oup.com/pages/standard-publication-reuse-rights"],"url":[{"@id":"https://academic.oup.com/jimmunol/article-pdf/151/10/5354/62222786/5354.pdf"}],"createdAt":"2022-12-31","modifiedAt":"2025-03-30","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360002215928796416","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Development and validation of a lateral flow assay for the detection of crustacean protein in processed 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Urticaria."},{"@language":"ja","@value":"魚類による接触じん麻疹における原因抗原の検討"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001204427763072","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Identification of tropomyosin as a major allergen in the octopus Octopus vulgaris and elucidation of its IgE-binding epitopes."}]},{"@id":"https://cir.nii.ac.jp/crid/1390001206415851264","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"ja","@value":"魚貝類アレルゲンに関する食品化学的研究"},{"@language":"en","@value":"Food-chemical studies on allergens of fish and shellfish"},{"@language":"ja-Kana","@value":"ギョカイルイ アレルゲン ニ カンスル ショクヒン カガクテキ ケンキュウ"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001206472407296","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Purification and IgE-Binding Epitopes of a Major Allergen 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adsorption of proteins from pink shrimp (Pandalus eous) onto stainless steel surfaces"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282681453639936","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Immunostimulation Effects of Yellowtail Heart Extracts in Vitro and in Vivo"},{"@value":"Immunostimulation Effects of Yellowtail Heart Extracts<i>in Vitro</i>and<i>in Vivo</i>"}]},{"@id":"https://cir.nii.ac.jp/crid/1390285300183228160","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Crustaceans and 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