Background: Characterization of the primary structure of allergens is a prerequisite for the design of new diagnostic and therapeutic tools for allergic diseases. Objective: The purpose of this study was the identification and characterization of a low-molecular-weight, IgE-binding, bee venom (BV) allergen. Methods: BV proteins were separated by using size exclusion chromatography and HPLC. IgE antibody binding to purified proteins was analyzed by means of immunoblotting, and T-cell response was analyzed by means of proliferation assay. Amino acid sequence was determined with 2 approaches, namely Edman degradation and carboxy terminal analysis with mass spectrometry. Results: Api m 6, which migrated as an 8-kd band in SDS-PAGE, was frequently (42%) recognized by IgE from BV-hypersensitive patients. In addition, PBMCs from BV-hypersensitive patients, as well as from a normal control subject, proliferated in response to this allergen. Api m 6 exists as 4 isoforms of 7190, 7400, 7598, and 7808 d, respectively. Amino acid sequences obtained from HPLC-purified preparations revealed that the isoforms were constituted of a common central core of 67 residues, only differing in the amino- and carboxy-terminal ends. Api m 6 showed no significant sequence homology with known proteins. Conclusions: We have identified and sequenced a new BV allergen that elicits a strong IgE and T-cell response in a large number of BV-hypersensitive patients. Api m 6 should be considered in the diagnostic and therapeutic approach of BV immunotherapy on the basis of peptides or recombinant proteins.
CITATION STYLE
Kettner, A., Hughes, G. J., Frutiger, S., Astori, M., Roggero, M., Spertini, F., & Corradin, G. (2001). Api m 6: A new bee venom allergen. Journal of Allergy and Clinical Immunology, 107(5 SUPPL.), 914–920. https://doi.org/10.1067/mai.2001.113867
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