TY - JOUR
T1 - Purification and characterisation of relevant natural and recombinant apple allergens
AU - Oberhuber, Christina
AU - Ma, Yan
AU - Marsh, Justin
AU - Rigby, Neil
AU - Smole, Ursula
AU - Radauer, Christian
AU - Alessandri, Stefano
AU - Briza, Peter
AU - Zuidmeer, Laurian
AU - Maderegger, Bernhard
AU - Himly, Martin
AU - Sancho, Ana I.
AU - Van Ree, Ronald
AU - Knulst, André
AU - Ebner, Christof
AU - Shewry, Peter
AU - Mills, E. N Clare
AU - Wellner, Klaus
AU - Breiteneder, Heimo
AU - Hoffmann-Sommergruber, Karin
AU - Bublin, Merima
N1 - , Biotechnology and Biological Sciences Research Council, United Kingdom
PY - 2008/11
Y1 - 2008/11
N2 - 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. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.
AB - 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. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.
KW - Apple
KW - Apple allergens
KW - Food allergens
KW - Malus domestica
KW - PR proteins
U2 - 10.1002/mnfr.200700522
DO - 10.1002/mnfr.200700522
M3 - Article
C2 - 18683825
SN - 1613-4125
VL - 52
SP - S208-S219
JO - Molecular Nutrition and Food Research
JF - Molecular Nutrition and Food Research
IS - 2
ER -