Cereals & Grains Association
Log In

Deduced Amino Acid Sequence of an α-Gliadin Gene from Spelt Wheat (Spelta) Includes Sequences Active in Celiac Disease

July 1999 Volume 76 Number 4
Pages 548 — 551
Donald D. Kasarda 1 , 2 and Renato D'Ovidio 3

U. S. Department of Agriculture, Agricultural Research Service, Western Regional Research Center, 800 Buchanan Street, Albany, CA 94710-1105. Corresponding author. Phone: 510/559-5687. E-mail: kasarda@pw.usda.gov Dipartimento di Agrobiologia e Agrochimica, Università degli Studi della Tuscia, Via S. Camillo de Lellis, 0100 Viterbo, Italy.

Go to Article:
Accepted April 19, 1999.

The complete amino acid sequence of an α-type gliadin from spelt wheat (spelta) has been deduced from the cloned DNA sequence and compared with α-type gliadin sequences from bread wheat. The comparison showed only minor differences in amino acid sequences between the α-type gliadin from bread wheat and the α-type gliadin from spelta. The two sequences had an identity of 98.5%. Larger differences can be found between different α-type gliadin amino acid sequences from common bread wheat. Because all the different classes of gliadins, α, β, γ, and ω, appear to be active in celiac disease, it is reasonably certain that the spelta gliadin is also toxic. We conclude that spelta is not a safe grain for people with celiac disease, contrary to the implications in labeling a bread made from spelta as “an alternative to wheat”. Our conclusions are in accord with spelta and bread wheat being classed taxonomically as subspecies of the same genus and species, Triticum aestivum L.

This article is in the public domain and not copyrightable. It may be freely reprinted with customary crediting of the source. American Association of Cereal Chemists, Inc., 1999.