References/Publications for Western/Immunoblot of Ara h 8

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18727014 Mol Nutr Food Res. 2008 Nov;52 Suppl 2:S272-85. doi: 10.1002/mnfr.200700524.

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

Marsh J(1), Rigby N, Wellner K, Reese G, Knulst A, Akkerdaas J, van Ree R,
Radauer C, Lovegrove A, Sancho A, Mills C, Vieths S, Hoffmann-Sommergruber K,
Shewry PR.

23495786 J Agric Food Chem. 2013 Apr 17;61(15):3714-25. doi: 10.1021/jf305347r. Epub 2013
Apr 8.

Analysis of crude protein and allergen abundance in peanuts (Arachis hypogaea cv.
Walter) from three growing regions in Australia.

Walczyk NE(1), Smith PM, Tovey E, Wright GC, Fleischfresser DB, Roberts TH.

24057594 Biol Chem. 2014 Feb;395(2):239-50. doi: 10.1515/hsz-2013-0206.

Roasting and lipid binding provide allergenic and proteolytic stability to the
peanut allergen Ara h 8.

Petersen A, Rennert S, Kull S, Becker WM, Notbohm H, Goldmann T, Jappe U.

Abstract Ara h 8 is the peanut allergen homologous to the birch pollen allergen
Bet v 1. Because Bet v 1 has been shown to bind lipophilic ligands, the aim of
this investigation was to determine the impact of lipid binding and roasting on
the Ara h 8 structure and their influences on allergenicity. For the
characterization of natural Ara h 8 (nAra h 8) from roasted and unroasted
peanuts, circular dichroism spectroscopy, hydrophobic binding assay,
immunohistochemistry, and immunoblot with sera of peanut allergic patients were
performed and compared with results from recombinant Ara h 8 (rAra h 8) and Bet v
rAra h 8 displayed stronger hydrophobicity than rBet v 1. Patients' sera
showed IgE reactivity with rAra h 8 and nAra h 8 from roasted peanuts, whereas
fewer sera recognized nAra h 8 from unroasted peanuts. Simulated gastric
digestion experiments demonstrated low proteolytic stability of rAra h 8, whereas
the stability of nAra h 8 was increasingly higher in unroasted and roasted
peanuts. The results demonstrate that IgE reactivity and thermal and proteolytic
stability are reinforced in nAra h 8 after roasting, most likely due to Maillard
reactions, lipid oxidations, and lipophilic associations. These aspects must be
considered when estimating the allergenicity of Bet v 1-homologous proteins.

DOI: 10.1515/hsz-2013-0206
PMID: 24057594 [Indexed for MEDLINE]