Epitopes described in "Antigenicity of the oligosaccharide moiety of the Japanese cedar (Cryptomeria japonica) pollen allergen, Cry jI."

Reference
Article Authors:A Hijikata; I Matsumoto; K Kojima; H Ogawa
Article Title:Antigenicity of the oligosaccharide moiety of the Japanese cedar (Cryptomeria japonica) pollen allergen, Cry jI.
Reference Detail
Reference ID:1005305
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.
Affiliations:Department of Chemistry, Faculty of Science, Ochanomizu University, Tokyo, Japan.
Date:1994
Reference Type:Literature
PubMed ID:7920021
Journal:Int Arch Allergy Immunol
Journal Volume:105
Article Pages:198-202
Journal ISSN:1423-0097
Article Chemical List:Allergens;Antigens, Plant;Cry j I protein, Cryptomeria japonica;Lectins;Oligosaccharides;Plant Lectins;Plant Proteins
Article MeSH List:Allergens(immunology); Animals; Antigens, Plant; Carbohydrate Sequence; Cross Reactions; Enzyme-Linked Immunosorbent Assay; Humans; Immunoblotting; Lectins; Molecular Sequence Data; Oligosaccharides(chemistry; immunology); Plant Lectins; Plant Proteins(immunology); Pollen(immunology); Rabbits
Curation Last Updated:2014-09-11 20:03:29