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Proteome and phosphoproteome of Africanized and European honeybee venoms

Authors

  • Virgínia Maria Ferreira Resende,

    1. Division of Clinical Immunology and Allergy, Department of Medicine, University of São Paulo, São Paulo, SP, Brazil
    2. Institute for Investigation in Immunology (iii-INCT), São Paulo, SP, Brazil
    3. MPI of Molecular Cell Biology and Genetics, Dresden, Germany
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  • Andrej Vasilj,

    1. MPI of Molecular Cell Biology and Genetics, Dresden, Germany
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  • Keity Souza Santos,

    1. Division of Clinical Immunology and Allergy, Department of Medicine, University of São Paulo, São Paulo, SP, Brazil
    2. Institute for Investigation in Immunology (iii-INCT), São Paulo, SP, Brazil
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  • Mario Sergio Palma,

    1. Institute for Investigation in Immunology (iii-INCT), São Paulo, SP, Brazil
    2. Institute of Biosciences of Rio Claro, Sao Paulo State University (UNESP), Rio Claro, SP, Brazil
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  • Andrej Shevchenko

    Corresponding author
    • MPI of Molecular Cell Biology and Genetics, Dresden, Germany
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  • Colour Online: See the article online to view Figs. 1 and 2 in colour.

Correspondence: Dr. Andrej Shevchenko, MPI of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany

E-mail: shevchenko@mpi-cbg.de

Fax: +49-351-210-2000

Abstract

Honey bee venom toxins trigger immunological, physiological, and neurological responses within victims. The high occurrence of bee attacks involving potentially fatal toxic and allergic reactions in humans and the prospect of developing novel pharmaceuticals make honey bee venom an attractive target for proteomic studies. Using label-free quantification, we compared the proteome and phosphoproteome of the venom of Africanized honeybees with that of two European subspecies, namely Apis mellifera ligustica and A. m. carnica. From the total of 51 proteins, 42 were common to all three subspecies. Remarkably, the toxins melittin and icarapin were phosphorylated. In all venoms, icarapin was phosphorylated at the 205Ser residue, which is located in close proximity to its known antigenic site. Melittin, the major toxin of honeybee venoms, was phosphorylated in all venoms at the 10Thr and 18Ser residues. 18Ser phosphorylated melittin—the major of its two phosphorylated forms—was less toxic compared to the native peptide.

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