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Biological Chemistry

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Volume 395, Issue 2

Issues

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

Arnd Petersen
  • Corresponding author
  • 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
  • These authors contributed equally to this work.
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/ Sandra Rennert
  • 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
  • These authors contributed equally to this work.
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/ Skadi Kull
  • 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
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/ Wolf-Meinhard Becker
  • 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
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/ Holger Notbohm
  • Department of Virology and Molecular Biology, University of Lübeck, Ratzeburger Allee 160, D-23538 Lübeck, Germany
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/ Torsten Goldmann
  • Division of Clinical and Experimental Pathology, Research Center Borstel, Airway Research Center North (ARCN), Member of the German Center for Lung Research, Borstel, Parkallee 3, D-23845 Borstel, Germany
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/ Uta Jappe
  • 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
  • Department of Dermatology, University of Lübeck, Ratzeburger Allee 160, D-23538 Lübeck, Germany
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Published Online: 2013-09-20 | DOI: https://doi.org/10.1515/hsz-2013-0206

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.

Keywords: Ara h 8; Bet v 1 homologue; gastric and pancreatic digestion; lipophilic allergens; peanut allergy

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About the article

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:


Received: 2013-06-18

Accepted: 2013-09-13

Published Online: 2013-09-20

Published in Print: 2014-02-01


Citation Information: Biological Chemistry, Volume 395, Issue 2, Pages 239–250, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/hsz-2013-0206.

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