Homology modelling of the major peanut allergen Ara h 2 and surface mapping of IgE-binding epitopes
Autor: | Pierre Rougé, Raphaël Culerrier, Annick Barre, Jean-Philippe Borges |
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Rok vydání: | 2005 |
Předmět: |
Models
Molecular Nut Arachis Molecular Sequence Data Immunology Molecular Conformation Cross Reactions Biology medicine.disease_cause Immunoglobulin E Protein Structure Secondary Homology (biology) Epitope Allergen food Botany medicine Immunology and Allergy Storage protein Amino Acid Sequence Glycoproteins Plant Proteins chemistry.chemical_classification digestive oral and skin physiology food and beverages Allergens Antigens Plant food.food Epitope mapping chemistry Biochemistry biology.protein Sequence Alignment Epitope Mapping 2S Albumins Plant Brazil nut |
Zdroj: | Immunology Letters. 100:153-158 |
ISSN: | 0165-2478 |
DOI: | 10.1016/j.imlet.2005.03.014 |
Popis: | Three-dimensional models built for the peanut Ara h 2 allergen and other structurally-related 2S albumin allergens of dietary nuts exhibited an overall three-dimensional fold stabilized by disulphide bridges well conserved among all the members of the 2S albumin superfamily. Conformational analysis of the linear IgE-binding epitopes mapped on the molecular surface of Ara h 2 showed no structural homology with the corresponding regions of the walnut Jug r 1, the pecan nut Car i 1 or the Brazil nut Ber e 1 allergens. The absence of epitopic community does not support the allergenic cross-reactivity observed between peanut and walnut or Brazil nut, which presumably depends on other ubiquitous seed storage protein allergens, namely the vicilins. However, the major IgE-binding epitope identified on the molecular surface of the walnut Jug r 1 allergen shared a pronounced structural homology with the corresponding region of the pecan nut Car i 1 allergen. With the exception of peanut, 2S albumins could thus account for the IgE-binding cross-reactivity observed between some other dietary nuts, e.g. walnut and pecan nut. |
Databáze: | OpenAIRE |
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