An immunological study of wheat gluten proteins and derivatives

Abstract

Sera from subjects with proven gliadin-induced celiac disease were used to make immunological comparisons of wheat gluten, glutenin, gliadin, gliadin derivatives, and gliadin components. The antigenic behavior of gliadin proteins was closely associated with their native structure. Although for a single antigen, Gli I, a precise folding of the protein chains may not be essential for activity, the random coil form of the antigen is inactive. In addition, antigenicity is influenced by the type of polar end-groups on aspartic and glutamic acid residues in gliadin. The Gli I antigen, which commonly elicits a precipitin response in subjects with gluten-induced celiac disease but rarely does so in other subjects, was also closely associated with certain gliadin components.