Purification and characterisation of relevant natural and recombinant apple allergens

A - Papers appearing in refereed journals

Oberhuber, C., Ma, Y., Marsh, J., Rigby, N., Smole, U., Radauer, C., Alessandri, S., Briza, P., Zuidmeer, L., Maderegger, B., Himly, M., Sancho, A. I., Van Ree, R., Knulst, A., Ebner, C., Shewry, P. R., Mills, E. N. C., Wellner, K., Breiteneder, H., Hoffmann-Sommergruber, K. and Bublin, M. 2008. Purification and characterisation of relevant natural and recombinant apple allergens. Molecular Nutrition & Food Research. 52, pp. S208-S219.

AuthorsOberhuber, C., Ma, Y., Marsh, J., Rigby, N., Smole, U., Radauer, C., Alessandri, S., Briza, P., Zuidmeer, L., Maderegger, B., Himly, M., Sancho, A. I., Van Ree, R., Knulst, A., Ebner, C., Shewry, P. R., Mills, E. N. C., Wellner, K., Breiteneder, H., Hoffmann-Sommergruber, K. and Bublin, M.
Abstract

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.

KeywordsFood Science & Technology
Year of Publication2008
JournalMolecular Nutrition & Food Research
Journal citation52, pp. S208-S219
Digital Object Identifier (DOI)doi:10.1002/mnfr.200700522
PubMed ID18683825
Open accessPublished as non-open access
Funder project or codeCGI
FunderBiotechnology and Biological Sciences Research Council
European Union - EU
Austrian Science Fund
ISSN16134125
PublisherWiley
Grant IDFOOD-CT-2005-514000
SFB-F01802

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