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Licensed Unlicensed Requires Authentication Published by De Gruyter September 20, 2013

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

  • Arnd Petersen EMAIL logo , Sandra Rennert , Skadi Kull , Wolf-Meinhard Becker , Holger Notbohm , Torsten Goldmann and Uta Jappe
From the journal Biological Chemistry

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 1. 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.


Corresponding author: Arnd Petersen, Division of Clinical and Molecular Allergology, Research Center Borstel, Airway Research Center North (ARCN), Member of the German Center for Lung Research, Parkallee 22, D-23845 Borstel, Germany, e-mail:

Parts of this project were kindly supported by the Kanert Foundation for Allergy Research and by the Deutsche Forschungsgemeinschaft (SFB/TR22 Z01). The excellent technical support of Marisa Böttger, Markus Hartmann, Daniela Warneke, and Jasmin Tiebach is gratefully acknowledged.

Conflict of interest statement

The authors declare to have no financial/commercial conflicts of interest.

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Received: 2013-06-18
Accepted: 2013-09-13
Published Online: 2013-09-20
Published in Print: 2014-02-01

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