Immunological Characterization of Honey Proteins and Identification of MRJP 1 as an IgE-Binding Protein
| Autor: | Nobue Takamatsu, Takashi Arita, Takashi Nakashima, Takeshi Hayashi |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
food.ingredient
Galectin 3 Blotting Western Molecular Sequence Data Immunoglobulin E Applied Microbiology and Biotechnology Biochemistry Epitope Analytical Chemistry Epitopes food Japan Immunoblot Analysis Royal jelly Animals Humans Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Amino Acid Sequence Molecular Biology Peptide sequence chemistry.chemical_classification biology Binding protein Fatty Acids Organic Chemistry food and beverages Honey General Medicine Allergens Bees Peptide Fragments chemistry Child Preschool biology.protein Insect Proteins Electrophoresis Polyacrylamide Gel Female Antibody Glycoprotein Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 75:556-560 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.100778 |
| Popis: | We encountered a fourth case of honey allergy in Japan. We characterized and identified the IgE-binding proteins in honey using the serum of a honey-allergenic patient. Immunoblot analysis revealed that IgE in the patient serum specifically bound to four proteins in each honey sample. At least three of these IgE-binding proteins were N-linked glycoproteins. To identify the 60-kDa IgE-binding protein in dandelion honey, the N-terminal sequences of the fragmented protein were analyzed, revealing the protein to be major royal jelly protein 1 (MRJP 1). Three IgE-binding proteins removed of N-linked oligosaccharide showed a large reduction in IgE-binding activity as compared with the intact protein. This suggests that the carbohydrates in the IgE-binding proteins are a major epitope for patient IgE. |
| Databáze: | OpenAIRE |
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