Please use this identifier to cite or link to this item:
Title: Proteome and phosphoproteome of Africanized and European honeybee venoms
Authors: RESENDE, Virginia Maria FerreiraVASILJ, AndrejSANTOS, Keity SouzaPALMA, Mario SergioSHEVCHENKO, Andrej
Citation: PROTEOMICS, v.13, n.17, p.2638-2648, 2013
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 (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.
Appears in Collections:

Artigos e Materiais de Revistas Científicas - FM/Outros
Outros departamentos - FM/Outros

Artigos e Materiais de Revistas Científicas - LIM/60
LIM/60 - Laboratório de Imunologia Clínica e Alergia

Files in This Item:
File Description SizeFormat 
  Restricted Access
publishedVersion (English)470.14 kBAdobe PDFView/Open Request a copy

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.