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Purification and characterisation of a panel of peanut allergens suitable for use in allergy diagnosis

Authors :
Justin T. Marsh
Clare Mills
Jaap H. Akkerdaas
André C. Knulst
Peter R. Shewry
Ana I. Sancho
Christian Radauer
Ronald van Ree
Stefan Vieths
Gerald Reese
Alison Lovegrove
Karin Hoffmann-Sommergruber
Neil M. Rigby
Klaus Wellner
Amsterdam institute for Infection and Immunity
Experimental Immunology
Amsterdam Public Health
Source :
Molecular nutrition & food research, 52(Suppl. 2), S272-S285. Wiley-VCH Verlag
Publication Year :
2008

Abstract

Peanut is a major cause of type 1 hypersensitive reactions including anaphylaxis. This results from the presence of a number of protein allergens, six of which are being studied as part of the EU FP6 EuroPrevall programme. These are Ara h 1 (7S globulin), Ara h 2, Ara h 6 (2S albumins), Ara h 3/4 (11S globulins) and Ara h 8 (Bet v 1 homologue). Methods for the purification of Ara h 1, Ara h 3/4, Ara h 2 and Ara h 6 from peanut seeds and for the production of recombinant Ara h 8 in Escherichia coli are described with spectroscopic analyses being used to confirm that they are authentically folded. N-terminal sequencing of the proteins purified from peanut seeds also revealed details of the differences between isoforms and their generation by proteolytic processing within the seed. Preliminary IgE binding studies of the purified allergens confirmed that they retained their immunological properties indicating their suitability for use in allergy diagnosis.

Details

ISSN :
16134133 and 16134125
Volume :
52
Database :
OpenAIRE
Journal :
Molecular nutritionfood research
Accession number :
edsair.doi.dedup.....003d8052e6d6d686f0f87fe63d8e9c52