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Molecular and immunological characterization of -component (Onc k 5), a major IgE-binding protein in chum salmon roe
Title: | Molecular and immunological characterization of -component (Onc k 5), a major IgE-binding protein in chum salmon roe |
Authors: | Shimizu, Yutaka Browse this author →KAKEN DB | Kishimura, Hideki Browse this author →KAKEN DB | Kanno, Gaku Browse this author | Nakamura, Atsushi Browse this author | Adachi, Reiko Browse this author →KAKEN DB | Akiyama, Hiroshi Browse this author →KAKEN DB | Watanabe, Kazuhiko Browse this author | Hara, Akihiko Browse this author →KAKEN DB | Ebisawa, Motohiro Browse this author | Saeki, Hiroki Browse this author →KAKEN DB |
Keywords: | β′-component | IgE-binding ability | recombinant allergen | salmon roe allergy | vitellogenin |
Issue Date: | Mar-2014 |
Publisher: | Oxford University Press |
Journal Title: | International Immunology |
Volume: | 26 |
Issue: | 3 |
Start Page: | 139 |
End Page: | 147 |
Publisher DOI: | 10.1093/intimm/dxt051 |
PMID: | 24215907 |
Abstract: | Molecular characterization of a major allergen from salmon roe.Salmon roe has a high allergic potency and often causes anaphylaxis in Japan. The major allergic protein of salmon roe is β′-component, which is a 35kDa vitellogenin fragment consisting of two subunits. To elucidate structural information and immunological characteristics, β′-component and the subunit components were purified from chum salmon (Onchorhincus keta) roe and vitellogenin-encoding mRNA was used to prepare β′-component subunit-encoding cDNA. This was PCR-amplified, cloned and sequenced and the deduced amino acid sequence compared with partial sequences of β′-component obtained by peptide mapping. The recombinant β′-component subunit was produced by bacterial expression in Escherichia coli and its IgE-binding ability was measured by ELISA using the sera of a patient allergic to salmon roe. This was then compared with that of the native β′-component with and without carboxymethylation. Following successful cloning of the cDNA encoding the β′-component subunit, 170 amino acid residues were deduced and matched with the amino acid sequences of 121 and 88 residues in the 16kDa and 18kDa subunits, respectively. The sequences of both β′-component subunits were almost identical, and the predicted secondary structure of the β′-component showed a high content of -pleated sheets and no -helices. There was no difference in IgE-binding ability between the native and recombinant β′-component subunits at the same protein concentration, regardless of carboxymethylation. In conclusion, β′-component is a homodimer protein composed of two isoform subunits having the same level of IgE-binding ability and, therefore, allergenic identity. |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/57341 |
Appears in Collections: | 水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 佐伯 宏樹
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