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Biosci Rep. 2018 Feb 14. pii: BSR20171245. doi: 10.1042/BSR20171245. [Epub ahead of print]

A modified, hypoallergenic variant of the  Ricinus communis Ric c1 protein retains biological activity.

Author information

1
Biosciences and Biotechnology, Northern State University of Rio de Janeiro - Darcy Ribeiro (UENF), Av. Alberto Lamego, 2000, Campos dos Goytacazes, 28013602, Brazil.
2
Biosciences and Biotechnology, Northern State University of Rio de Janeiro - Darcy Ribeiro (UENF), Av. Alberto Lamego, 2000, Campos dos Goytacazes, 28013602, Brazil olga@uenf.br.

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.

KEYWORDS:

Ricinus communis; allergies; hypoallergern; immunoterapy; mutation

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