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Mol Immunol. 2015 Feb;63(2):449-55. doi: 10.1016/j.molimm.2014.09.018. Epub 2014 Oct 17.

IgE recognition of chimeric isoforms of the honeybee (Apis mellifera) venom allergen Api m 10 evaluated by protein array technology.

Author information

1
Laboratory of Molecular Entomology and Bee Pathology, Ghent University, Krijgslaan 281 S2, B-9000 Ghent, Belgium.
2
Allergy Research Group, Department of Dermatology, University Medical Center Freiburg, Hauptstrasse 7, D-79104 Freiburg, Germany.
3
Center of Allergy and Environment (ZAUM), Technical University and Helmholtz Center Munich, Ingolstädter Landstraße 1, D-85764 Munich, Germany.
4
Department of Engineering, Aarhus University, Gustav Wieds Vej 10, DK-8000 Aarhus C, Denmark.
5
Department of Immunology, Allergology, and Rheumatology, University of Antwerp, Universiteitsplein 1, B-2610 Antwerp, Belgium.
6
Laboratory of Protein Biochemistry and Biomolecular Engineering, Ghent University, K.L. Ledeganckstraat 35, B-9000 Ghent, Belgium.
7
Laboratory of Molecular Entomology and Bee Pathology, Ghent University, Krijgslaan 281 S2, B-9000 Ghent, Belgium. Electronic address: Dirk.deGraaf@UGent.be.

Abstract

Api m 10 has recently been established as novel major allergen that is recognized by more than 60% of honeybee venom (HBV) allergic patients. Previous studies suggest Api m 10 protein heterogeneity which may have implications for diagnosis and immunotherapy of HBV allergy. In the present study, RT-PCR revealed the expression of at least nine additional Api m 10 transcript isoforms by the venom glands. Two distinct mechanisms are responsible for the generation of these isoforms: while the previously known variant 2 is produced by an alternative splicing event, novel identified isoforms are intragenic chimeric transcripts. To the best of our knowledge, this is the first report of the identification of chimeric transcripts generated by the honeybee. By a retrospective proteomic analysis we found evidence for the presence of several of these isoforms in the venom proteome. Additionally, we analyzed IgE reactivity to different isoforms by protein array technology using sera from HBV allergic patients, which revealed that IgE recognition of Api m 10 is both isoform- and patient-specific. While it was previously demonstrated that the majority of HBV allergic patients display IgE reactivity to variant 2, our study also shows that some patients lacking IgE antibodies for variant 2 display IgE reactivity to two of the novel identified Api m 10 variants, i.e. variants 3 and 4.

KEYWORDS:

Allergy; Chimeric transcripts; Honeybee; Protein array; Venom

PMID:
25451974
DOI:
10.1016/j.molimm.2014.09.018
[Indexed for MEDLINE]

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