Journal
PROTEOMICS
Volume 13, Issue 17, Pages 2638-2648Publisher
WILEY
DOI: 10.1002/pmic.201300038
Keywords
Animal proteomics; Apis mellifera; Honeybee venom; LC-MS; MS; Melittin; Phosphorylation
Funding
- Deutscher Akademischer Austausch Dienst (DAAD)
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
- Instituto Nacional de Ciencia e Tecnologia (INCT)
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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 (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 melittinthe major of its two phosphorylated formswas less toxic compared to the native peptide.
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