Jump to ContentJump to Main Navigation
Show Summary Details
More options …

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

See all formats and pricing
More options …
Volume 395, Issue 2


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.
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ 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.
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ 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
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ 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
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Holger Notbohm
  • Department of Virology and Molecular Biology, University of Lübeck, Ratzeburger Allee 160, D-23538 Lübeck, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ 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
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ 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
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2013-09-20 | DOI: https://doi.org/10.1515/hsz-2013-0206


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


  • Abdullah, M., Schultz, H., Kähler, D., Branscheid, D., Dalhoff, K., Zabel, P., Vollmer, E., and Goldmann, T. (2009). Expression of the acute phase protein haptoglobin in human lung cancer and tumor-free lung tissues. Pathol. Res. Pract. 205, 639–647.Google Scholar

  • Beyer, K., Morrow, E., Li, X.M., Bardina, L., Bannon, G.A., Burks, A.W., and Sampson, H.A. (2001). Effects of cooking methods on peanut allergenicity. J. Allergy Clin. Immunol. 107, 1077–1081.Google Scholar

  • Blake, M.S., Johnston, K.H., Jone, G.J., and Gotschlich, E.C. (1984). A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots. Anal. Biochem. 136, 175–179.Google Scholar

  • Bock, S.A., Muñoz-Furlong, A., and Sampson, H.A. (2001). Fatalities due to anaphylactic reactions to foods. J. Allergy Clin. Immunol. 107, 191–193.Google Scholar

  • Boldt, A., Fortunato, D., Conti, A., Petersen, A., Ballmer-Weber, B., Lepp, U., Reese, G., and Becker, W.M. (2005). Analysis of the composition of an immunoglobulin E reactive high molecular weight protein complex of peanut extract containing Ara h 1 and Ara h 3/4. Proteomics 5, 675–686.Google Scholar

  • Bufe, A., Spangfort, M.D., Kahlert, H., Schlaak, M., and Becker, W.M. (1996). The major birch pollen allergen, Bet v 1, shows ribonuclease activity. Planta 199, 413–415.Google Scholar

  • Carrin, M.E. and Carelli, A.A. (2010). Peanut oil: compositional data. Eur. J. Lipid Sci. Technol. 112, 697–707.Google Scholar

  • Chadha, P. and Das, R.H. (2006). A pathogenesis related protein, AhPR10 from peanut: an insight of its mode of antifungal activity. Planta 225, 213–222.Google Scholar

  • Chung, S.Y., Maleki, S., Champagne, E.T., Buhr, K.L., and Gorbet, D.W. (2002). High-oleic peanuts are not different from normal peanuts in allergenic properties. J. Agric. Food Chem. 50, 878–882.Google Scholar

  • D’Andréa, S., Jolivet, P., Boulard, C., Larré, C., Froissard, M., and Chardot, T. (2007). Selective one-step extraction of Arabidopsis thaliana seed oleosins using organic solvents. J. Agric. Food Chem. 55, 10008–10015.Google Scholar

  • Dohil, M.A., Alvarez-Connelly, E., and Eichenfield, L.F. (2009). Fluochinolone acetonide 0.01% in peanut oil: safety and efficacy data in the treatment of childhood atopic dermatitis in infants as young as 3 months of age. Pediatr. Dermatol. 26, 262–268.Google Scholar

  • Du Toit, G., Katz, Y., Sasieni, P., Mesher, D., Maleki, S.J., Fisher, H.R., Fox, A.T., Turcanu, V., Amir, T., Zadik-Mnuhin, G., et al. (2008). Early consumption of peanuts in infancy is associated with a low prevalence of peanut allergy. J. Allergy Clin. Immunol. 122, 984–991.Google Scholar

  • Ebner, C., Hirschwehr, R., Bauer, L., Breiteneder, H., Valenta, R., Ebner, H., Kraft, D., and Scheiner, O. (1995). Identification of allergens in fruits and vegetables: IgE cross-reactivities with the important birch pollen allergens Bet v 1 and Bet v 2 (birch profilin). J. Allergy Clin. Immunol 95, 962–969.Google Scholar

  • Fernandes, H., Michalska, K., Sikorski, M., and Jaskolski M. (2013). Structural and functional aspects of PR-10 proteins. FEBS J. 280, 1169–1199.Google Scholar

  • Ferreira, F., Hirtenlehner, K., Jilek, A., Godnik-Cvar, J., Breiteneder, H., Grimm, R., Hoffmann-Sommergruber, K., Scheiner, O., Kraft, D., Breitenbach, M., et al. (1996). Dissection of immunoglobulin E and T lymphocyte reactivity of isoforms of the major birch pollen allergen Bet v 1: potential use of hypoallergenic isoforms for immunotherapy. J. Exp. Med. 183, 599–609.Google Scholar

  • Görg, A., Weiss, W., and Dunn, M.J. (2004). Current two-dimensional electrophoresis technology for proteomics. Proteomics 4, 3665–3685.PubMedCrossrefGoogle Scholar

  • Gupta, R.S., Springston, E.E., Warrier, M.R., Smith, B., Kumar, R., Pongracic, J., and Holl, J.L. (2011). The prevalence, severity, and distribution of childhood food allergy in the United States. Pediatrics 128, e9–17.Google Scholar

  • Hancock, K. and Tsang, V.C. (1983). India ink staining of proteins on nitrocellulose paper. Anal. Biochem. 133, 157–162.Google Scholar

  • Heukeshoven, J. and Dernick, R. (1988). Improved silver staining procedure for fast staining in PhastSystem Development Unit. I. Staining of sodium dodecyl sulfate gels. Electrophoresis 9, 28–32.Google Scholar

  • Ho, M.H., Lee, S.L., Wong, W.H., Ip, P., and Lau, Y.L. (2012). Prevalence of self-reported food allergy in Hong Kong children and teens – a population survey. Asian Pac. J. Allergy Immunol. 30, 275–284.Google Scholar

  • Kleine-Tebbe, J., Wangorsch. A., Vogel, L., Crowell, D.N., Haustein, U.F., and Vieths, S. (2002). Severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1-related PR-10 protein in soybean, SAM 22. J. Allergy Clin. Immunol. 110, 797–804.Google Scholar

  • Kosma, P., Sjölander, S., Landgren, E., Borres, P., and Hedlin, G. (2010). Severe reactions after intake of soy drink in birch pollen-allergic children sensitized to Gly m 4. Acta Pediatr. 100, 305–307.Google Scholar

  • Kyhse-Andersen, J. (1984). Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J. Biochem. Biophys. Methods 10, 203–209.Google Scholar

  • Lack, G., Fox, D., Northstone, K., and Golding, J. (2003). Factors associated with the development of peanut allergy in childhood. N. Engl. J. Med. 348, 977–985.Google Scholar

  • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685.Google Scholar

  • Liu, X., Jin, Q., Liu, Y., Huang, J., Wang, X., Mao, W., and Wang, S. (2011). Changes in volatile compounds of peanut oil during the roasting process for production of aromatic roasted peanut oil. J. Food Sci. 76, C404–C412.Google Scholar

  • Louis-Jeune, C., Andrade-Navarro, M.A., and Perez-Iratxeta, C. (2012). Prediction of protein secondary structure from circular dichroism using theoretically derived spectra. Proteins 80, 374–381.Google Scholar

  • Maleki, S.J., Chung, S.Y., Champagne, E.T., and Raufman, J.P. (2000a). The effects of roasting on the allergenic properties of peanut proteins. J. Allergy Clin. Immunol. 106, 763–768.Google Scholar

  • Maleki, S.J., Kopper, R.A., Shin, D.S., Park, C.W., Compadre, C.M., Sampson, H., Burks, A.W., and Bannon, G.A. (2000b). Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation. J. Immunol. 164, 5844–5849.Google Scholar

  • Maleki, S.J., Viquez, O., Jacks, T., Dodo, H., Champagne, E.T., Chung, S.Y., and Landry, S.J. (2003). The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function. J. Allergy Clin. Immunol. 112, 190–195.Google Scholar

  • Markovic-Housley, Z., Degano, M., and Lamba, D. (2003). Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier. J. Mol. Biol. 325, 123–133.Google Scholar

  • Mattila, K. and Renkonen, R. (2009). Modelling of Bet v 1 binding to lipids. Scand. J. Immunol. 70, 116–124.Google Scholar

  • Mills, E.N., Jenkins, J.A., Alcocer, M.J., and Shewry, P.R. (2004). Structural, biological, and evolutionary relationships of plant food allergens sensitizing via the gastrointestinal tract. Crit. Rev. Food Sci. Nutr. 44, 379–407.Google Scholar

  • Mittag, D., Akkerdaas, J., Ballmer-Weber, B.K., Vogel, L., Wensing, M., Becker, W.M., Koppelman, S.J., Knulst, A.C., Helbling, A., Hefle, S.L., et al. (2004a). Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy. J. Allergy Clin. Immunol. 114, 1410–1417.Google Scholar

  • Mittag, D., Vieths, S., Vogel, L., Becker, W.M., Rihs, H.P., Helbling, A., Wüthrich, B., and Ballmer-Weber, B.K. (2004b). Soybean allergy in patients allergic to birch pollen: clinical investigation and molecular characterization of allergens. J. Allergy Clin. Immunol. 113, 148–154.Google Scholar

  • Mogensen, J.E., Wimmer, R., Larsen, J.N., Spangfort, M.D., and Otzen, D.E. (2002). The major birch allergen Bet v 1 shows affinity for a broad spectrum of physiological ligands. J. Biol. Chem. 277, 23684–23692.Google Scholar

  • Mondoulet, L., Paty, E., Drumare, M.F., Ah-Leung, S., Scheinmann, P., Willemot, R.M., Wal, J.M., and Bernard, H. (2005). Influence of thermal processing on the allergenicity of peanut proteins. J. Agric. Food Chem. 53, 4547–4553.Google Scholar

  • Olszewski, A., Pons, L., Moutété, F., Aimone-Gastin, I., Kanny, G., Moneret-Vautrin, D.A., and Guéant, J.L. (1998). Isolation and characterization of proteic allergens in refined peanut oil. Clin. Exp. Allergy 28, 850–859.Google Scholar

  • Özcan, M.M. (2010). Some nutritional characteristics of kernel and oil of peanut (Arachis hypogaea L.). J. Oleo Sci. 59, 1–5.Google Scholar

  • Pali-Schöll, I., Herzog, R., Wallmann, J., Szalai, K., Brunner, R., Lukschal, A., Karagiannis, P., Diesner, S.C., and Jensen-Jarolim, E. (2010). Antacids and dietary supplements with an influence on the gastric pH increase the risk for food sensitization. Clin. Exp. Allergy 40, 1091–1098.Google Scholar

  • Petersen, A., Bufe, A., Schlaak, M., and Becker, W.M. (1995). Characterization of the allergen group VI in timothy grass pollen (Phl p 6). I. Immunological and biochemical studies. Int. Arch. Allergy Immunol. 108, 49–54.Google Scholar

  • Petersen, A., Dresselhaus, T., Grobe, K., and Becker, W.M. (2006). Proteome analysis of maize pollen for allergy-relevant components. Proteomics 6, 6317–6325.CrossrefPubMedGoogle Scholar

  • Rajashankar, K., Bufe, A., Weber, W., Eschenburg, S., Lindner, B., and Betzel, C. (2002). Structure of the functional domain of the major grass-pollen allergen Phl p 5b. Acta Crystallogr. D. Biol. Crystallogr. 58, 1175–1781.Google Scholar

  • Ramazzotti, M., Mulinacci, N., Pazzagli, L., Moribondo, M., Manao, G., Vincieri, F.F., and Degl’Innocenti, D. (2008). Analytic investigations on protein content in refined seed oils: implications in food allergy. Food Chem. Toxicol. 46, 3383–3388.Google Scholar

  • Rennert, S., Krause, S., Becker, W.M., and Petersen, A. (2012). Lipids modify structure and digestibility of peanut allergen Ara h 8. In: Environmental and Genetic Factors in Allergy and Clinical Immunology. Proceedings of the 27th Symposium of the Collegium Internationale Allergologicum (CIA), R. van Ree, J. Ring, and G. Marone, eds. (Pisa: Pacini Editore), pp. 241–243.Google Scholar

  • Riecken, S., Lindner, B., Petersen, A., Jappe, U., and Becker, W.M. (2008). Purification and characterization of natural Ara h 8, the Bet v 1 homologous allergen from peanut, provides a novel isoform. Biol. Chem. 389, 415–423.Google Scholar

  • Sancho, A.I., Wangorsch, A., and Jensen, B.M. (2011). Responsiveness of the major birch allergen Bet v 1 scaffold to the gastric environment: impact on structure and allergenic activity. Mol. Nutr. Food Res. 55, 1690–1699.Google Scholar

  • Schimek, E.M., Zwölfer, B., Briza, P., Jahn-Schmid, B., Vogel, L., Vieths, S., Ebner, C., and Bohle, B. (2005). Gastrointestinal digestion of Bet v 1-homologous food allergens destroys their mediator-releasing, but not T cell-activating, capacity. J. Allergy Clin. Immunol. 116, 1327–1333.Google Scholar

  • Sicherer, S.H., Muñoz-Furlong, A., and Sampson, H.A. (2003). Prevalence of peanut and tree nut allergy in the United States determined by means of a random digit dial telephone survey: a 5-year follow-up study. J. Allergy Clin. Immunol. 112, 1203–1207.Google Scholar

  • Strid, J., Hourihane, J., Kimbert, I., Callard, R., and Strobel, S. (2005). Epicutaneous exposure to peanut protein prevents oral tolerance and enhances allergic sensitization. Clin. Exp. Allergy 35, 757–766.Google Scholar

  • Suphioglu, C., Singh, M.B., Taylor, P., Bellomo, R., Holmes, P., Puy, R., and Knox, R.B. (1992). Mechanism of grass-pollen-induced asthma. Lancet 339, 569–572.Google Scholar

  • Vissers, Y.M., Blanc, F., Skov, P.S., Johnson, P.E., Rigby, N.M., Przybylski-Nicaise, L., Bernard, H., Wal, J.M., Ballmer-Weber, B., Zuidmeer-Jongejan, L., et al. (2011). Effect of heating and glycation on the allergenicity of 2S albumins (Ara h 2/6) from peanut. PLoS One 6, e23998.Google Scholar

  • Zhai, H., Ramirez, R.G., and Maibach, H.I. (2003). Hydrating effects of a corticoid oil formulation and its vehicle on human skin. Skin Pharmacol. Appl. Skin Physiol. 16, 367–371.Google Scholar

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.

Export Citation

©2014 by Walter de Gruyter Berlin Boston.Get Permission

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

Carina Rib-Schmidt, Philipp Riedl, Veronika Meisinger, Luisa Schwaben, Thomas Schulenborg, Andreas Reuter, Dirk Schiller, Christian Seutter von Loetzen, and Paul Rösch
Molecular Nutrition & Food Research, 2018, Page 1700886
Chiara Palladino and Heimo Breiteneder
Molecular Immunology, 2018
Judith Pekar, Davide Ret, and Eva Untersmayr
Molecular Immunology, 2018
Beatriz Cabanillas, Uta Jappe, and Natalija Novak
Molecular Nutrition & Food Research, 2017, Page 1700446
Beatriz Cabanillas and Natalija Novak
Critical Reviews in Food Science and Nutrition, 2017, Page 00
Uta Jappe and Christian Schwager
Current Allergy and Asthma Reports, 2017, Volume 17, Number 9
Manuel Gómez del Moral and Eduardo Martínez-Naves
Immune Network, 2017, Volume 17, Number 3, Page 133
Christian Schwager, Skadi Kull, Jochen Behrends, Niels Röckendorf, Frauke Schocker, Andreas Frey, Arne Homann, Wolf-Meinhard Becker, and Uta Jappe
Journal of Allergy and Clinical Immunology, 2017
Andrea Wangorsch, Annette Jamin, Jonas Lidholm, Nora Gräni, Claudia Lang, Barbara Ballmer-Weber, Stefan Vieths, and Stephan Scheurer
Molecular Nutrition & Food Research, 2017, Volume 61, Number 4, Page 1600902
Heide Havenith, Karolin Kern, Paul Rautenberger, Holger Spiegel, Michael Szardenings, Elke Ueberham, Jörg Lehmann, Matthias Buntru, Simon Vogel, Regina Treudler, Rainer Fischer, and Stefan Schillberg
Biotechnology Journal, 2017, Volume 12, Number 2, Page 1600441
Magnus P. Borres, Nobuyuki Maruyama, Sakura Sato, and Motohiro Ebisawa
Allergology International, 2016, Volume 65, Number 4, Page 378
A. Angelina, S. Sirvent, C. Palladino, A. Vereda, J. Cuesta-Herranz, T. Eiwegger, R. Rodríguez, H. Breiteneder, M. Villalba, and O. Palomares
Allergy, 2016, Volume 71, Number 9, Page 1284
Syed Umer Abdullah, Yuri Alexeev, Philip E. Johnson, Neil M. Rigby, Alan R. Mackie, Balvinder Dhaliwal, and E. N. Clare Mills
Scientific Reports, 2016, Volume 6, Number 1
Arnd Petersen, Skadi Kull, Sandra Rennert, Wolf-Meinhard Becker, Susanne Krause, Martin Ernst, Thomas Gutsmann, Johann Bauer, Buko Lindner, and Uta Jappe
Journal of Allergy and Clinical Immunology, 2015, Volume 136, Number 5, Page 1295
Susanne Glaumann, Caroline Nilsson, S G O Johansson, Anna Asarnoj, Magnus Wickman, Magnus P Borres, and Anna Nopp
Clinical and Molecular Allergy, 2015, Volume 13, Number 1
Elana Lavine and Moshe Ben-Shoshan
Allergy, Asthma & Clinical Immunology, 2015, Volume 11, Number 1, Page 2
Merima Bublin, Thomas Eiwegger, and Heimo Breiteneder
Journal of Allergy and Clinical Immunology, 2014, Volume 134, Number 3, Page 521
Merima Bublin and Heimo Breiteneder
Current Allergy and Asthma Reports, 2014, Volume 14, Number 4

Comments (0)

Please log in or register to comment.
Log in