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Insect stings can cause life-threatening IgE-mediated anaphylactic reactions in venom-allergic patients. Although several compounds have already been described as venom allergens, prominent allergen candidates especially in the higher m.w. range have still remained elusive. Tandem mass spectrometry-based sequencing assigned a candidate gene to the most prominent putative high m.w. allergen Api m 5 (allergen C) in honeybee (Apis mellifera) venom and also allowed identification of its homologue Ves v 3 in yellow jacket (Vespula vulgaris) venom. Both proteins exhibit a pronounced sequence identity to human dipeptidyl peptidase IV or CD26. Reactivity of a human IgE mAb verified the presence of these proteins in the venoms. Both proteins were produced in insect cells and characterized for their enzymatic activity as well as their allergenic potential using sera and basophils from insect venom-allergic patients. Both Api m 5 and Ves v 3 were recognized by specific IgE of the majority of patients even in the absence of cross-reactive carbohydrate determinants. Serologic IgE reactivity closely matched activation of human basophils by Api m 5 or Ves v 3, thus underlining their relevance in functional assays. With Api m 5 and Ves v 3, a new pair of homologous allergens becomes available for future clinical applications in diagnosis and therapy that may also contribute to the understanding of molecular mechanisms of insect venoms. Moreover, the patient IgE reactivity together with the cellular activation demonstrates for the first time the relevance of high m.w. allergens in the context of hymenoptera venom allergy.

Original publication

DOI

10.4049/jimmunol.0803709

Type

Journal article

Journal

Journal of immunology (Baltimore, Md. : 1950)

Publication Date

05/2010

Volume

184

Pages

5403 - 5413

Addresses

Department of Chemistry, Institute of Biochemistry and Molecular Biology, University of Hamburg, Germany.

Keywords

Animals, Humans, Bees, Wasps, Spodoptera, Insect Bites and Stings, Immunoglobulin E, Insect Proteins, Recombinant Proteins, Bee Venoms, Wasp Venoms, Allergens, Amino Acid Sequence, Molecular Sequence Data, Dipeptidyl Peptidase 4