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| Article Authors: | A Hijikata; I Matsumoto; K Kojima; H Ogawa |
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| Article Title: | Antigenicity of the oligosaccharide moiety of the Japanese cedar (Cryptomeria japonica) pollen allergen, Cry jI. |
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| Reference ID: | 1005305 |
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| 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. |
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| Affiliations: | Department of Chemistry, Faculty of Science, Ochanomizu University, Tokyo, Japan. |
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| Date: | 1994 |
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| Reference Type: | Literature |
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| PubMed ID: | 7920021 |
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| Journal: | Int Arch Allergy Immunol |
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| Journal Volume: | 105 |
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| Article Pages: | 198-202 |
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| Journal ISSN: | 1423-0097 |
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| Article Chemical List: | Allergens;Antigens, Plant;Cry j I protein, Cryptomeria japonica;Lectins;Oligosaccharides;Plant Lectins;Plant Proteins |
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| 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 |
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| Curation Last Updated: | 2013-05-11 20:02:10 |
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