Immunochemical analysis of oat avenins in an oat cultivar and landrace collection

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http://hdl.handle.net/10138/318954

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Ahola , H G , Sontag-Strohm , T , Schulman , A , Tanhuanpää , P , Viitala , S & Huang , X 2020 , ' Immunochemical analysis of oat avenins in an oat cultivar and landrace collection ' , Journal of Cereal Science , vol. 95 , 103053 . https://doi.org/10.1016/j.jcs.2020.103053

Title: Immunochemical analysis of oat avenins in an oat cultivar and landrace collection
Author: Ahola, Hanna Gabriela; Sontag-Strohm, Tuula; Schulman, Alan; Tanhuanpää, Pirjo; Viitala, Sirja; Huang, Xin
Contributor: University of Helsinki, Department of Food and Nutrition
University of Helsinki, Department of Food and Nutrition
University of Helsinki, Viikki Plant Science Centre (ViPS)
University of Helsinki, Department of Food and Nutrition
Date: 2020-09
Language: eng
Number of pages: 8
Belongs to series: Journal of Cereal Science
ISSN: 0733-5210
URI: http://hdl.handle.net/10138/318954
Abstract: Oats have been found to be tolerated by most celiac disease patients, and oats are generally considered a good and safe addition to the gluten-free diet. There have been claims that some individual oat cultivars are harmful or immunogenic for celiac disease patients. In this study, we investigated 26 oat cultivars and landraces from the current breeding market and literature. Their total protein content ranged from 15.3% to 23.1% of which avenins ranged from 6.8% to 10.9%. Immunological activities of avenins were evaluated using mmunochemical analyses using monoclonal antibodies (mAb) R5 and G12. No immunological activity of the oat cultivars was observed by mAb R5 either in immunoblotting or enzyme-linked immunosorbent assay (ELISA). mAB G12 showed no activity in immunoblotting, but gave responses between 13 and 53 mg/kg in ELISA for total avenin extract. To understand the varying G12 activity, avenins were further fractionated. One avenin fraction showed a higher G12 response than the other fractions. Protein sequence comparison suggests that there is no direct binding to avenin-specific T-cell epitopes but the differences in repetitive regions in avenins may contribute to varying results in G12 ELISA.
Subject: 1182 Biochemistry, cell and molecular biology
avenin
gluten-free
ELISA
G12
prolamin
Gluten-free
G12
Prolamin
ELISA
PROTEIN
DISEASE
INTOLERANCE
EPITOPES
PEPTIDE
GLIADIN
WHEAT
DIET
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