Purification and characterisation of relevant natural and recombinant apple allergens
| Autor: | Ana I. Sancho, E. N. Clare Mills, Justin T. Marsh, Neil M. Rigby, Stefano Alessandri, Christof Ebner, Martin Himly, Karin Hoffmann-Sommergruber, André C. Knulst, Peter Briza, Christian Radauer, Yan Ma, Merima Bublin, Ursula Smole, Bernhard Maderegger, Ronald van Ree, Klaus Wellner, Laurian Zuidmeer, Peter R. Shewry, Heimo Breiteneder, Christina Oberhuber |
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| Přispěvatelé: | Amsterdam institute for Infection and Immunity, Experimental Immunology, Amsterdam Public Health |
| Předmět: |
Malus
medicine.disease_cause law.invention Allergen Antigen Food allergy law Botany medicine Humans Escherichia coli Plant Proteins biology Allergens Antigens Plant Immunoglobulin E biology.organism_classification medicine.disease Recombinant Proteins Biochemistry Profilin Food Science & Technology biology.protein Recombinant DNA Carrier Proteins Plant lipid transfer proteins Food Science Biotechnology |
| Zdroj: | Molecular nutrition & food research, 52(Suppl. 2), S208-S219. Wiley-VCH Verlag |
| ISSN: | 1613-4125 |
| DOI: | 10.1002/mnfr.200700522 |
| Popis: | Apple (Malus domestica) is the most widely cultivated fruit crop in Europe and frequently causes allergic reactions with a variable degree of severity. So far, four apple allergens Mal d 1, Mal d 2, Mal d 3 and Mal d 4 have been identified. Mal d 1, a Bet v 1 related allergen, and Mal d 4, apple profilin, are sensitive to proteolytic degradation, whereas Mal d 2, a thaumatin-like protein and Mal d 3, a nonspecific lipid transfer protein, are rather stable to proteolytic processes. Mal d 1 and Mal d 4 were purified after expression in Escherichia coli expression system, while Mal d 2 and Mal d 3 were purified from apple fruit tissue. All purified proteins were subjected to detailed physicochemical characterisation to confirm their structural integrity and maintained IgE binding capacity. Detailed investigations of carbohydrate moieties of Mal d 2 demonstrated their involvement in the overall IgE binding capacity of this allergen. It was concluded that the folded structure and IgE binding capacity of all four allergens were preserved during purification. |
| Databáze: | OpenAIRE |
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