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Plants 2018, 7(4), 101;

Wheat ATI CM3, CM16 and 0.28 Allergens Produced in Pichia Pastoris Display a Different Eliciting Potential in Food Allergy to Wheat

Department of Agriculture and Forest Science (DAFNE), University of Tuscia, Via S. C. de Lellis snc, 01100 Viterbo, Italy
Present address: Department of Land, Environment, Agriculture and Forestry (TESAF), University of Padova, Viale dell’Università 16, 35020 Legnaro (PD), Italy
UR 1268 BIA (Biopolymers, Interactions, Assemblies) INRA, 44300 Nantes, France
Aix Marseille Univ, CNRS, Centrale Marseille, iSm2, Marseille, France
Service d’Allergologie - CHU ANGERS, 4 rue Larrey 49933 Angers Cedex 9, France
Present address: Institute of Plant and Microbial Biology, Academia Sinica, Taipei, Taiwan
These authors equally contributed to the paper. Specifically, S.T. performed heterologous protein expression and purification, and R.L. performed the characterization of the patients’ sera, ELISA and degranulation tests.
This paper is dedicated to the dear memory of Prof. Renato D’Ovidio.
Author to whom correspondence should be addressed.
Received: 17 October 2018 / Revised: 7 November 2018 / Accepted: 15 November 2018 / Published: 16 November 2018
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Although wheat is a staple food for most of the human population, some of its components trigger adverse reactions. Among wheat components, the alpha-amylase/trypsin inhibitors (ATI) are important triggers of several allergies and activators of innate immunity. ATI are a group of exogenous protease inhibitors and include several polypeptides. The three ATI polypeptides named CM3, CM16 and 0.28 are considered major allergens, and might also play a role in other common wheat-related pathologies, such as Non Celiac Wheat Sensitivity and even Celiac Disease. On this basis, we pointed to obtain high amounts of them in purity and to evaluate their allergenicity potential. We thus isolated the mRNA corresponding to the three ATI genes CM3, CM16 and 0.28 from 28 days post-anthesis wheat kernels and the corresponding cDNAs were used for heterologous expression in Pichia pastoris. The three purified proteins were tested in degranulation assay against human sera of patients with food allergy to wheat. A large range of degranulation values was observed for each protein according to the sera tested. All of the three purified proteins CM3, CM16 and 0.28 were active as allergens because they were able to induce basophils degranulation on wheat allergic patients’ sera, with the highest values of β-hexosaminidase release observed for CM3 protein. View Full-Text
Keywords: wheat; alpha-amylase/trypsin inhibitor; heterologous expression; Pichia pastoris; allergy wheat; alpha-amylase/trypsin inhibitor; heterologous expression; Pichia pastoris; allergy

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Tundo, S.; Lupi, R.; Lafond, M.; Giardina, T.; Larré, C.; Denery-Papini, S.; Morisset, M.; Kalunke, R.; Sestili, F.; Masci, S. Wheat ATI CM3, CM16 and 0.28 Allergens Produced in Pichia Pastoris Display a Different Eliciting Potential in Food Allergy to Wheat . Plants 2018, 7, 101.

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