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Paramyosin from the Disc Abalone Haliotis Discus Discus
Author(s) -
Suzuki Midori,
Shimizu Keiko,
Kobayashi Yukihiro,
Ishizaki Shoichiro,
Shiomi Kazuo
Publication year - 2014
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/jfbc.12072
Subject(s) - abalone , haliotis discus , tropomyosin , recombinant dna , biology , complementary dna , allergen , myofibril , biochemistry , fishery , gene , myosin , allergy , immunology
Abstract Besides tropomyosin that represents a major allergen in mollusks as well as in crustaceans, a 100‐kDa allergen was recently found in the disc abalone Haliotis discus discus and identified as paramyosin, an invertebrate‐specific myofibrillar protein. In this study, the amino acid sequence (860 residues) of disc abalone paramyosin was elucidated by cDNA cloning. As high as 70% amino acid sequence homology was recognized between disc abalone and M editerranean mussel paramyosins, supporting the previously suggested immunoglobulin E (IgE) cross‐reactivity between both paramyosins. Disc abalone paramyosin was expressed in E scherichia coli as a HisGln ( HQ )‐tagged protein. As analyzed by enzyme‐linked immunosorbent assay, the recombinant preparation was judged to have almost the same IgE ‐binding ability as its natural counterpart. Practical Applications This study showed that sufficient amounts of the recombinant disc abalone paramyosin can be obtained in a relatively short time whenever needed. The recombinant disc abalone paramyosin is comparable in IgE ‐binding ability to the natural counterpart and hence could be used as an alternative antigen of the natural counterpart for molecular studies and diagnosis of mollusk allergy.