Abstract:
:Ric c1, an allergenic protein from Ricinus communis , is an insect α-amylase inhibitor that has become an occupational allergen. Ric c1 can cross-react with allergens from wheat, soybean, peanut, shrimp, fish, gluten, house dust, tobacco, and air fungus, thereby amplifying the concern and risks caused by Ricinus allergens. Two continuous IgE-binding epitopes were identified in Ric c1, both containing glutamic acid residues involved in IgE-binding and allergic challenges. We produced recombinant Ric c1 (rRic c1) in Escherichia coli , using primers from foliar R. communis DNA, and a mutant (Glu-Leu) recombinant protein (mrRic c1) in the same system using synthetic genes. rRic c1 preserved both allergenic and α-amylase inhibitory properties, and mrRic c1 drastically reduced allergenic properties. These results can help to establish meaningful relationships between structure, defense and allergenicity, important steps for producing engineered plants and developing new approaches for immunotherapy.
journal_name
Biosci Repjournal_title
Bioscience reportsauthors
Pacheco-Soares T,de Oliveira Carvalho A,da Silva Araújo J,de Souza GDS,Machado OLTdoi
10.1042/BSR20171245subject
Has Abstractpub_date
2018-02-14 00:00:00eissn
0144-8463issn
1573-4935pii
BSR20171245pub_type
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journal_title:Bioscience reports
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pub_type: 杂志文章,收录出版
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doi:10.1042/BSR20180367
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journal_title:Bioscience reports
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doi:10.1042/BSR20191609
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doi:10.1042/BSR20140083
更新日期:2014-07-04 00:00:00
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journal_title:Bioscience reports
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doi:10.1042/BSR20180568
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doi:10.1007/BF01117435
更新日期:1985-01-01 00:00:00
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journal_title:Bioscience reports
pub_type: 传,历史文章
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journal_title:Bioscience reports
pub_type: 杂志文章
doi:10.1042/BSR20181658
更新日期:2019-03-22 00:00:00
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journal_title:Bioscience reports
pub_type: 杂志文章
doi:10.1007/BF01122726
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pub_type: 杂志文章
doi:10.1007/BF01119901
更新日期:1985-10-01 00:00:00