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 A. m. 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 205 Ser 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 10 Thr and 18 Ser residues. 18 Ser
phosphorylated melittin - the major of its two phosphorylated forms -was less
toxic compared to the native peptide.
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