Antigenicity of the oligosaccharide moiety of the Japanese cedar (Cryptomeria japonica) pollen allergen, Cry jI

Int Arch Allergy Immunol. 1994 Oct;105(2):198-202. doi: 10.1159/000236826.

Abstract

Cry jI, a major allergenic glycoprotein of Cryptomeria japonica (Japanese cedar, Sugi), is the most common pollen allergen in Japan. Carbohydrate analysis and lectin staining indicated that Cry jI possesses the fucose/xylose-containing N-linked oligosaccharide which previously has been found in some plant glycoproteins. Rabbit polyclonal anti-Cry jI IgG antibodies were found to be highly cross-reactive with two other plant glycoproteins which have the same type of oligosaccharides, and the cross-reactivities were completely abolished on chemical deglycosylation of the glycoproteins. Enzyme-linked immunosorbent assay inhibition showed that the majority (up to 70%) of the anti-Cry jI rabbit IgG antibodies recognized the oligosaccharide moiety of Cry jI. The carbohydrate epitopes were found to be only partially involved in the binding of specific IgE antibodies from a pool of human patient sera.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens / immunology*
  • Animals
  • Antigens, Plant
  • Carbohydrate Sequence
  • Cross Reactions
  • Enzyme-Linked Immunosorbent Assay
  • Humans
  • Immunoblotting
  • Lectins
  • Molecular Sequence Data
  • Oligosaccharides / chemistry
  • Oligosaccharides / immunology*
  • Plant Lectins
  • Plant Proteins / immunology*
  • Pollen / immunology*
  • Rabbits

Substances

  • Allergens
  • Antigens, Plant
  • Cry j I protein, Cryptomeria japonica
  • Lectins
  • Oligosaccharides
  • Plant Lectins
  • Plant Proteins