Keywords

Cultivated Einkorn Wheat, Alpha, Gliadin, Gene Cloning, Celiac Disease, Phylogeny

Abstract

Alpha gliadin is the most consumed protein in people’s lives. Since it contains the main toxic peptide component that causes celiac disease (CD), it is also the most active protein that causes CD. In order to understand the potential of eel wheat in wheat quality breeding, a pair of ¦Á-gliadin specific primers was used to clone a new ¦Á-gliadin gene from cultivated eel wheat using genomic PCR. A total fragment size of 856 to 882 bp was obtained. The four gene sequences are named AA6, AA8, AA9 and AA21 (GenBank accession numbers are JN831382~JN831385). Among them, AA8, AA9 and AA21 all have a C¡úT substitution at position 102, resulting in the appearance of a TAG terminator and become pseudogenes; AA6 consists of 882 nucleotides and can encode 293 amino acids, which has the highest homology with known genes. It is 99%. It is inferred that the amino acid sequence has the typical structure of ¦Á-gliadin and is a new member of the ¦Á-gliadin family. CD toxic peptide analysis of AA6 showed that, except for the toxic peptides glia¦Á and glia¦Á2, which are not found in the A genome, the other seven known toxic peptides were distributed. Homology analysis of AA6 and 86 ¦Á-gliadins derived from wheat and its ancestral donor species showed that ¦Á-gliadin genes have differences in genome origin. Among them, ¦Á-gliadin genes derived from A and D genomes The similarity is high.

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Original research done by Li Yuge, Xing Ranran, Li Suoping

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