Abstract
Of the allergens identified to date, the major birch pollen allergen, Bet v 1, is of crucial importance in molecular allergology. First identified as an allergen in 1988, Bet v 1 has attained a key role in both basic and clinical research. Many structurally similar (homologous) molecules in tree pollen from the Fagales order, as well as from plant-derived foods, have been identified as related allergens. From an allergological perspective, Bet v 1 and its homologs are among the most important pollen allergens in the upper Northern hemisphere and the most common triggers of pollen-associated food allergies in adolescence and adulthood in areas of birch pollen exposure. Therefore, both Bet v 1 and its related allergens play an important role in our understanding of cross-reactivity, diagnostics, counseling, and allergen-specific immunotherapy in allergy sufferers. The present chapter summarizes the most important characteristics and discusses in detail the clinical symptoms and patterns of allergic disease caused by Bet v 1 and its homologs. The chapter then goes on to describe the options for molecular diagnostics and their interpretation as the basis for individual counseling and treatment (allergen-specific immunotherapy).
The present chapter is based on, and modified from, an article by the authors published in 2010 in Allergo Journal (Kleine-Tebbe J, Ballmer-Weber B, Breiteneder H, Vieths S: Bet v 1 und Homologe: Verursacher der Baumpollenallergie und birkenpollenassoziierter Kreuzreaktionen. Allergo J 2010; 19: 462–463).
The authors gratefully thank Dr. Steve Love, PhD, Laguna Niguel, CA, USA, for reading the manuscript, helpful suggestions, and editorial assistance with the English translation.
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References
Ballmer-Weber BK, Hoffmann-Sommergruber K. Molecular diagnosis of fruit and vegetable allergy. Curr Opin Allergy Clin Immunol. 2011;11:229–35.
Ballmer-Weber BK, Skamstrup Hansen K, Sastre J, et al. Component-resolved in vitro diagnosis of carrot allergy in three different regions of Europe. Allergy. 2012;67:758–66.
Bauermeister K, Ballmer-Weber BK, Bublin M, et al. Assessment of component-resolved in vitro diagnosis of celeriac allergy. J Allergy Clin Immunol. 2009;124:1273–81.
Berkner H, Neudecker P, Mittag D, et al. Cross-reactivity of pollen and food allergens: soybean Gly m 4 is a member of the Bet v 1 superfamily and closely resembles yellow lupine proteins. Biosci Rep. 2009;29:183–92.
Berkner H, Seutter von Loetzen C, Hartl M, et al. Enlarging the toolbox for allergen epitope definition with an allergen-type model protein. PLoS One. 2014;9:e111691.
Bolhaar ST, Tiemessen MM, Zuidmeer L, et al. Efficacy of birch-pollen immunotherapy on cross-reactive food allergy confirmed by skin tests and double-blind food challenges. Clin Exp Allergy. 2004;34:761–9.
Bousquet PJ, Chinn S, Janson C, et al. Geographical variation in the prevalence of positive skin tests to environmental aeroallergens in the European Community Respiratory Health Survey I. Allergy. 2007;62:301–9.
Breiteneder H, Pettenburger K, Bito A, et al. The gene coding for the major birch pollen allergen Betv1, is highly homologous to a pea disease resistance response gene. EMBO J. 1989;8:1935–8.
Bublin M, Eiwegger T, Breiteneder H. Do lipids influence the allergic sensitization process? J Allergy Clin Immunol. 2014;134:521–9.
Chruszcz M, Ciardiello MA, Osinski T, et al. Structural and bioinformatic analysis of the kiwifruit allergen Act d 11, a member of the family of ripening-related proteins. Mol Immunol. 2013;56:794–803.
Cromwell O, Niederberger V, Horak F, et al. Clinical experience with recombinant molecules for allergy vaccination. Curr Top Microbiol Immunol. 2011;352:27–42.
D’Avino R, Bernardi ML, Wallner M, et al. Kiwifruit Act d 11 is the first member of the ripening-related protein family identified as an allergen. Allergy. 2011;66:870–7.
Gajhede M, Osmark P, Poulsen FM, et al. X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy. Nat Struct Biol. 1996;3:1040–5.
Gepp B, Lengger N, Bublin M, et al. Chimeras of Bet v 1 and Api g 1 reveal heterogeneous IgE responses in patients with birch pollen allergy. J Allergy Clin Immunol. 2014;134:188–94.
Guhsl EE, Hofstetter G, Hemmer W, et al. Vig r 6, the cytokinin-specific binding protein from mung bean (Vigna radiata) sprouts, cross-reacts with Bet v 1-related allergens and binds IgE from birch pollen allergic patients’ sera. Mol Nutr Food Res. 2014;58:625–34.
Haftenberger M, Laussmann D, Ellert U, et al. Prävalenz von Sensibilisierungen gegen Inhalations- und Nahrungsmittelallergene. Ergebnisse der Studie zur Gesundheit Erwachsener in Deutschland (DEGS1). Bundesgesundheitsblatt Gesundheitsforschung Gesundheitsschutz. 2013;56:687–97.
Hansen KS, Khinchi MS, Skov PS, et al. Food allergy to apple and specific immunotherapy with birch pollen. Mol Nutr Food Res. 2004;48:441–8.
Hurlburt BK, Offermann LR, McBride JK, et al. Structure and function of the peanut panallergen Ara h 8. J Biol Chem. 2013;288:36890–901.
Jenkins JA, Griffiths-Jones S, Shewry PR, et al. Structural relatedness of plant food allergens with specific reference to cross-reactive allergens: an in silico analysis. J Allergy Clin Immunol. 2005;115:163–70.
Kleine-Tebbe J, Herold D, Vieths S. Sojaallergie durch Kreuzreaktionen gegen Birkenpollen-Majorallergen Bet v 1. Allergologie. 2008;31:303–13.
Kleine-Tebbe J, Meißner A-M, Jappe U, et al. Allergenfamilien und molekulare Diagnostik IgE-vermittelter Nahrungsmittelallergien: von der Theorie zur Praxis. Allergo J. 2010;19:251–63.
Kleine-Tebbe J, Vogel L, Crowell DN, et al. Severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1- related PR-10 protein in soybean, SAM22. J Allergy Clin Immunol. 2002;110:797–804.
Markovic-Housley Z, Basle A, Padavattan S, et al. Structure of the major carrot allergen Dau c 1. Acta Crystallogr D Biol Crystallogr. 2009;65:1206–12.
Matricardi PM, Kleine-Tebbe J, Hoffmann HJ, Valenta R, Hilger C, Hofmaier S, Aalberse RC, Agache I, Asero R, Ballmer-Weber B, Barber D, Beyer K, Biedermann T, Biló MB, Blank S, Bohle B, Bosshard PP, Breiteneder H, Brough HA, Caraballo L, Caubet JC, Crameri R, Davies JM, Douladiris N, Ebisawa M, Eigenmann PA, Fernandez-Rivas M, Ferreira F, Gadermaier G, Glatz M, Hamilton RG, Hawranek T, Hellings P, Hoffmann-Sommergruber K, Jakob T, Jappe U, Jutel M, Kamath SD, Knol EF, Korosec P, Kuehn A, Lack G, Lopata AL, Mäkelä M, Morisset M, Niederberger V, Nowak-Wezgrzyn AH, Papadopoulos NG, Pastorello EA, Pauli G, Platts-Mills T, Posa D, Poulsen LK, Raulf M, Sastre J, Scala E, Schmid JM, Schmid-Grendelmeier P, van Hage M, van Ree R, Vieths S, Weber R, Wickman M, Muraro A, Ollert M. EAACI molecular allergology user’s guide. Pediatr Allergy Immunol. 2016;27 Suppl 23:1–250.
Mauro M, Russello M, Incorvaia C, et al. Birch-apple syndrome treated with birch pollen immunotherapy. Int Arch Allergy Immunol. 2011;156:416–22.
Neudecker P, Schweimer K, Nerkamp J, et al. Allergic cross-reactivity made visible: solution structure of the major cherry allergen Pru av 1. J Biol Chem. 2001;276:22756–63.
Osterballe M, Hansen TK, Mortz CG, et al. The clinical relevance of sensitization to pollen-related fruits and vegetables in unselected pollen-sensitized adults. Allergy. 2005;60:218–25.
Pasternak O, Bujacz GD, Fujimoto Y, et al. Crystal structure of Vigna radiata cytokinin-specific binding protein in complex with zeatin. Plant Cell. 2006;18:2622–34.
Radauer C, Lackner P, Breiteneder H. The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands. BMC Evol Biol. 2008;8:286.
Schirmer T, Hoffimann-Sommergrube K, Susani M, et al. Crystal structure of the major celery allergen Api g 1: molecular analysis of cross-reactivity. J Mol Biol. 2005;351:1101–9.
Schmitz R, Ellert U, Kalcklosch M, et al. Patterns of sensitization to inhalant and food allergens – findings from the German Health Interview and Examination Survey for Children and Adolescents. Int Arch Allergy Immunol. 2013;162:263–70.
Seutter von Loetzen C, Hoffmann T, Hartl MJ, et al. Secret of the major birch pollen allergen Bet v 1: identification of the physiological ligand. Biochem J. 2014;457:379–90.
van Hoffen E, Peeters KA, van Neerven RJ, et al. Effect of birch pollen-specific immunotherapy on birch pollen-related hazelnut allergy. J Allergy Clin Immunol. 2011;127:100–1.
Villalta D, Asero R. Is the detection of IgE to multiple Bet v 1-homologous food allergens by means of allergen microarray clinically useful? J Allergy Clin Immunol. 2010;125:1158–61.
Wangorsch A, Jamin A, Foetisch K, et al. Identification of Sola l 4 as Bet v 1 homologous pathogenesis related-10 allergen in tomato fruits. Mol Nutr Food Res. 2014;59:582–92.
Worm M, Jappe U, Kleine-Tebbe J, et al. Food allergies resulting from immunological cross-reactivity with inhalant allergens: guidelines from the German Society for Allergology and Clinical Immunology (DGAKI), the German Dermatology Society (DDG), the Association of German Allergologists (AeDA) and the Society for Pediatric Allergology and Environmental Medicine (GPA). Allergo J Int. 2014;23:1–16.
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Kleine-Tebbe, J., Ballmer-Weber, B.K., Breiteneder, H., Vieths, S. (2017). Bet v 1 and its Homologs: Triggers of Tree-Pollen Allergy and Birch Pollen-Associated Cross-Reactions. In: Kleine-Tebbe, J., Jakob, T. (eds) Molecular Allergy Diagnostics. Springer, Cham. https://doi.org/10.1007/978-3-319-42499-6_2
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