Melanie Albrecht, MSc, Yvonne Kühne, MSc, Barbara K

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Relevance of IgE binding to short peptides for the allergenic activity of food allergens Melanie Albrecht, MSc, Yvonne Kühne, MSc, Barbara K. Ballmer-Weber, MD, Wolf-Meinhard Becker, PhD, Thomas Holzhauser, PhD, Iris Lauer, PhD, Andreas Reuter, PhD, Stefanie Randow, Sabine Falk, Andrea Wangorsch, BSc, Jonas Lidholm, PhD, Gerald Reese, PhD, Stefan Vieths, PhD Journal of Allergy and Clinical Immunology Volume 124, Issue 2, Pages 328-336.e6 (August 2009) DOI: 10.1016/j.jaci.2009.05.031 Copyright © 2009 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Fig 1 IgE reactivity of different rAra h 2 preparations. A, CD spectra of native and denatured (red/alk) recombinant Ara h 2. B, IgE reactivity of sera from 2 individuals with peanut allergy with native rAra h 2 compared with denatured (red/alk) Ara h 2 was detected in Western blot analysis. Journal of Allergy and Clinical Immunology 2009 124, 328-336.e6DOI: (10.1016/j.jaci.2009.05.031) Copyright © 2009 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Fig 2 Identification of IgE-reactive peptides of Ara h 2 with epitope mapping of synthetic peptides on SPOT membrane. Chemiluminescence detection of pool serum of patient without allergy (NA) and sera of patient with peanut allergy, 163 and JG3. Journal of Allergy and Clinical Immunology 2009 124, 328-336.e6DOI: (10.1016/j.jaci.2009.05.031) Copyright © 2009 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Fig 3 Inhibition of IgE-binding with short peptides in ELISA with rAra h 2 and rPen a 1. Binding of IgE from patients' sera (A, JG3, 163; B, PI-1, PII-3) to allergens coated on microtiter plates (A, rAra h 2; B, rPen a 1) was inhibited by coincubation with the parent allergen (A, rAra h 2; B, rPen a 1), denatured allergen (A, red/alk rAra h 2) or synthetic short peptides representing the main sequential IgE-binding regions identified in this study. Journal of Allergy and Clinical Immunology 2009 124, 328-336.e6DOI: (10.1016/j.jaci.2009.05.031) Copyright © 2009 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Fig 4 Inhibition of mediator release from humanized RBL cells with short peptides. Mediator release from humanized RBL cells sensitized with human sera (A, JG3, 163; B, PI-1, PII-3) with (dashed line) or without (solid line) preincubation with short peptides representing the main sequential IgE-binding regions of the parent allergen (A, rAra h 2; B, rPen a 1) in response to the recombinant allergen (A, rAra h 2; B, rPen a 1). The dotted line in A reflects the mediator release in response to denatured rAra h 2. Journal of Allergy and Clinical Immunology 2009 124, 328-336.e6DOI: (10.1016/j.jaci.2009.05.031) Copyright © 2009 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Fig 5 Secondary structure of tropomyosin. Recombinant Pen a 1 (black, solid line), Pen a 1–hybrid (gray, long dashes) and mouse tropomyosin (black, short dashes) were applied to CD spectroscopy to confirm their secondary structure. Journal of Allergy and Clinical Immunology 2009 124, 328-336.e6DOI: (10.1016/j.jaci.2009.05.031) Copyright © 2009 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Fig 6 Inhibition of IgE binding to Pen a 1 in ELISA. Binding of IgE to rPen a 1 from patients' sera PI-1 (black circle) or PII-3 (gray triangle) was inhibited by coincubation with recombinant Pen a 1 (solid line), tropomyosin hybrid (dashed line), or recombinant murine tropomyosin (dotted line). Journal of Allergy and Clinical Immunology 2009 124, 328-336.e6DOI: (10.1016/j.jaci.2009.05.031) Copyright © 2009 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Amino acid sequence alignment of the allergen Pen a 1 (DQ151457), mouse α- tropomyosin, slow isoform (AAA03725), and the hybrid MusmTM_x_Pen_a_1. The major IgE-antibody binding regions of Pen a 1 and the homologous regions of mouse tropomyosin and the hybrid are shaded in gray. Journal of Allergy and Clinical Immunology 2009 124, 328-336.e6DOI: (10.1016/j.jaci.2009.05.031) Copyright © 2009 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Dot blot of soluble Ara h 2 peptides Dot blot of soluble Ara h 2 peptides. A, Distribution of soluble peptides on nitrocellulose membrane (50 μg/peptide). IgE immune detection of soluble Ara h 2 peptides with nonallergic serum pool (B) or serum from subject with peanut allergy 163 (C). Journal of Allergy and Clinical Immunology 2009 124, 328-336.e6DOI: (10.1016/j.jaci.2009.05.031) Copyright © 2009 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Dot -blot inhibition assay of IgE binding to soluble Ara h 2 peptides Dot -blot inhibition assay of IgE binding to soluble Ara h 2 peptides. Highly reactive soluble peptides of Ara h 2 were dotted on nitrocellulose membrane, and IgE binding of serum from subject with peanut allergy 163 was either not inhibited or inhibited with 250 μg of the respective peptide or 50 μg rAra h 2. Immune detection with a serum pool from patients without allergy served as control. neg., Negative. Journal of Allergy and Clinical Immunology 2009 124, 328-336.e6DOI: (10.1016/j.jaci.2009.05.031) Copyright © 2009 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Three -dimensional model of Ara h 2 Three -dimensional model of Ara h 2. The model was created with Swissmodel (swissmodel.expasy.org) on the basis of the known solution structure of Ara h 6 (1w2qA).E1 The location of IgE-binding areas identified in this study are shown in green (peptide 6), red (peptides 8-10), and pink (peptides 21-28). The figure was illustrated with the pdb-viewer program. Journal of Allergy and Clinical Immunology 2009 124, 328-336.e6DOI: (10.1016/j.jaci.2009.05.031) Copyright © 2009 American Academy of Allergy, Asthma & Immunology Terms and Conditions