Premium
Purification and characterisation of a panel of peanut allergens suitable for use in allergy diagnosis
Author(s) -
Marsh Justin,
Rigby Neil,
Wellner Klaus,
Reese Gerald,
Knulst André,
Akkerdaas Jaap,
van Ree Ronald,
Radauer Christian,
Lovegrove Alison,
Sancho Ana,
Mills Clare,
Vieths Stefan,
HoffmannSommergruber Karin,
Shewry Peter R.
Publication year - 2008
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.200700524
Subject(s) - peanut allergy , recombinant dna , escherichia coli , globulin , immunoglobulin e , allergen , allergy , chemistry , anaphylaxis , biology , immunology , biochemistry , food allergy , antibody , gene
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.