Api m 6: A new bee venom allergen

• Published in: Journal of allergy and clinical immunology Vol. 107; no. 5; pp. 914 - 920
• Main Authors: Kettner, Alexander, Hughes, Graham J., Frutiger, Séverine, Astori, Mireille, Roggero, Mario, Spertini, François, Corradin, Giampietro
• Format: Journal Article Conference Proceeding
• Language: English
• Published: New York, NY Mosby, Inc 01.05.2001; Elsevier
• Subjects: allergens; Allergens - immunology; Allergens - isolation & purification; Allergic diseases; Amino Acid Motifs; Amino Acid Sequence; Animals; Antibody Specificity; Antigens, Plant; Api m 6; Api m 6 antigen; Apis mellifera; bee venom; Bee Venoms - chemistry; Bee Venoms - immunology; Biological and medical sciences; carboxypeptidase; Chromatography, Gel; Chromatography, High Pressure Liquid; Humans; Hymenoptera; Hypersensitivity, Immediate - blood; Hypersensitivity, Immediate - immunology; IgE; Immunoglobulin E - blood; Immunoglobulin E - immunology; Immunopathology; immunotherapy; Insect Proteins - immunology; Insect Proteins - isolation & purification; Lymphocyte Activation; matrix-assisted laser desorption-ionization time of flight mass spectrometry; Medical sciences; Molecular Sequence Data; Protein Denaturation; Skin allergic diseases. Stinging insect allergies; T cells; T-Lymphocytes - immunology; VIT; RT; MALDI-TOF; DTT; IgE; matrix-assisted laser desorption-ionization time of flight mass spectrometry; PLA2; MW; T cells; carboxypeptidase; allergens; BV; Api m 6; SI; bee venom; immunotherapy; Hymenoptera; Human; Immunopathology; Allergy; Immune response; Bee; Insecta; Apis; Apidae; Primary structure; Identification; Cellular immunity; Characterization; Apoidea; Arthropoda; Venom; T-Lymphocyte; Invertebrata; Humoral immunity; Aminoacid sequence; Aculeata; Allergen
• ISSN: 0091-6749
• DOI: 10.1067/mai.2001.113867

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. (J Allergy Clin Immunol 2001;107:914-20.)