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J. Biol. Chem., Vol. 277, Issue 25, 22656-22661, June 21, 2002

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The Major Conformational IgE-binding Epitopes of Hevein (Hev b6.02) Are Identified by a Novel Chimera-based Allergen Epitope Mapping Strategy^*

Piia Karisola, Harri Alenius^§, Jari Mikkola^§, Nisse Kalkkinen^¶, Jari Helin^¶, Olli T. Pentikäinen, Susanna Repo, Timo Reunala^**, Kristiina Turjanmaa^**, Mark S. Johnson, Timo Palosuo, and Markku S. Kulomaa^§§

From the  Department of Biological and Environmental Science, University of Jyväskylä, P. O. Box 35 (YAB), FIN-40014 University of Jyvskyl, Finland, ^§ Finnish Institute of Occupational Health, Topeliuksenkatu 42 aA, FIN-00250 Helsinki, Finland, ^¶ Institute of Biotechnology, University of Helsinki, P. O. Box 56, FIN-00014 University of Helsinki, Helsinki, Finland,  Department of Biochemistry and Pharmacy, Åbo Akademi University, P. O. Box 66, FIN-20521 Turku, Finland, ^** University Hospital of Tampere, P. O. Box 2000, FIN-33521 Tampere, Finland, and  National Public Health Institute, Mannerheimintie 166, FIN-00300 Helsinki, Finland

A novel approach to localize and reconstruct conformational IgE-binding epitope regions of hevein (Hev b6.02), a major natural rubber latex allergen, is described. An antimicrobial protein (AMP) from the amaranth Amaranthus caudatus was used as an immunologically non-IgE-binding adaptor molecule to which terminal or central parts of hevein were fused. Hevein and AMP share a structurally identical core region but have different N-terminal and C-terminal regions. Only 1 of 16 hevein-allergic patients showed weak IgE binding to purified native or recombinant AMP. Chimeric AMP with the hevein N terminus was recognized by IgE from 14 (88%) patients, and chimeric AMP with the hevein C terminus was recognized by IgE from 6 (38%) patients. In contrast, chimeric AMP containing the hevein core region was recognized by IgE from only two patients. When both the N-terminal and C-terminal regions of hevein were fused with the AMP core, IgE from all 16 patients bound to the chimera. This chimera was also able to significantly inhibit (>70%) IgE binding to the native hevein. On the contrary, linear synthetic peptides corresponding to hevein regions in the AMP chimeras showed no significant IgE binding capacity in either enzyme-linked immunosorbent assay or inhibition enzyme-linked immunosorbent assay. These results suggest that the IgE binding ability of hevein is essentially determined by its N-terminal and C-terminal regions and that major IgE-binding epitopes of hevein are conformational. The chimera-based epitope mapping strategy described here provides a valuable tool for defining structural epitopes and creating specific reagents for allergen immunotherapy.

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