Molecular characterization of the IgE-binding epitopes in the fast ω-gliadins of Triticeae in relation to wheat-dependent, exercise-induced anaphylaxis

Gene. 2016 Oct 10;591(1):27-33. doi: 10.1016/j.gene.2016.06.040. Epub 2016 Jun 30.

Abstract

Fast ω-gliadins were minor components of wheat storage proteins but a major antigen triggering allergy to wheat. Sixty-six novel full-length fast ω-gliadin genes with unique characteristics were cloned and sequenced from wheat and its relative species using a PCR-based strategy. Their coding regions ranged from 177bp to 987bp in length and encoded 4.28kDa to 37.56kDa proteins. On the base of first three deduced amino acids at the N-terminal, these genes could be classified into the six subclasses of SRL-, TRQ-, GRL-, NRL-, SRP- and SRM-type ω-gliadin genes. Compared by multiple alignments, these genes were significantly different from each other, due to the insertion or deletion at the repetitive domain. An analysis of the IgE-binding epitopes of the 66 deduced fast ω-gliadins demonstrated that they contained 0-24 IgE-binding epitopes. The phylogenetic tree demonstrated that the fast ω-gliadins and slow ω-gliadins were separated into two groups and their divergence time was 21.64millionyears ago. Sequence data of the fast ω-gliadin genes assist in the study of the origins and evolutions of the different types of ω-gliadins while also providing a basis for the synthesis of monoclonal antibodies to detect wheat antigen content.

Keywords: Allergy; Fast ω-gliadin; IgE-binding epitopes; Triticum aestivum; Variation.

MeSH terms

  • Amino Acid Sequence
  • Anaphylaxis / etiology*
  • Anaphylaxis / immunology*
  • Cloning, Molecular
  • Epitopes / genetics*
  • Exercise*
  • Genes, Plant
  • Gliadin / chemistry
  • Gliadin / genetics*
  • Humans
  • Hypersensitivity / immunology
  • Immunoglobulin E / genetics*
  • Phylogeny
  • Polymerase Chain Reaction
  • Triticum / genetics*

Substances

  • Epitopes
  • Immunoglobulin E
  • Gliadin