期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 73, 期 4, 页码 840-848出版社
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.80751
关键词
shrimp allergy; Penaeus japonicus tropomyosin; cDNA cloning; recombinant protein; IgE-binding epitope
类别
资金
- Skylark Food Science Institute
- Ministry of Education. Culture, Sports. Science. and Technology of Japan
Tropomyosins have been identified as a common allergen in crustaceans, but their allergenicity is not well understood. In the present study, we isolated an allergen, Pen j 1, a tropomyosin from kuruma prawn Penaeus Japonicus, and determined its N-terminal amino acid sequence. The cDNA encoding the allergen was cloned by 5'- and 3'-rapid amplification of cDNA ends (RACE), and was found to code for a protein which consists of 284 amino acid residues. Sequencing analyses indicated for the first time that mature tropomyosm is formed by the elimination of a leader peptide of nine amino acid residues. To elucidate the binding sites of IgE antibodies in the sera of shrimp-sensitive patients, various recombinant peptides were expressed in Escherichia coli as fusion proteins with glutathione S-transferase (GST), and the examined with regard to reactivity with IgE antibodies. The IgE-binding epitopes were found to locate over the whole sequence of the allergen, and the IgE antibodies in the sera were found to recognize strongly its C-terminal region.
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