Evidence for novel tomato seed allergens: IgE-reactive legumin and vicilin proteins identified by multidimensional protein fractionation-mass spectrometry and in silico epitope modeling

J Proteome Res. 2009 Mar;8(3):1111-22. doi: 10.1021/pr800186d.

Abstract

Tomato fruit and seed allergens were detected by IgE-immunoblotting using sera from 18 adult tomato-sensitized patients selected based on a positive history skin prick test (SPT) and specific Immunglobulin (Ig) E-levels. Isolated tomato seed total protein showed high SPT activity comparable or even higher than tomato fruit protein. For the molecular characterization of tomato seed allergens, a multidimensional protein fractionation strategy and LC-MS/MS was used. Two legumin- and vicilin-proteins were purified and showed strong IgE-reactivity in immunoblots. Individual patient sera exhibited varying IgE-sensitivity against the purified proteins. In silico structural modeling indicates high homology between epitopes of known walnut allergens and the detected IgE-crossreactive tomato proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens / immunology*
  • Amino Acid Sequence
  • Chromatography, Liquid
  • Epitopes / immunology
  • Food Hypersensitivity / immunology
  • Humans
  • Immunoglobulin E / immunology*
  • Lycopersicon esculentum / immunology*
  • Models, Molecular
  • Molecular Sequence Data
  • Plant Proteins / immunology*
  • Protein Structure, Tertiary
  • Proteome / metabolism
  • Seed Storage Proteins / immunology*
  • Seeds / immunology*
  • Tandem Mass Spectrometry

Substances

  • Allergens
  • Epitopes
  • Plant Proteins
  • Proteome
  • Seed Storage Proteins
  • legumin protein, plant
  • Immunoglobulin E
  • vicilin protein, plant