Unraveling the venom proteome of the bumblebee (Bombus terrestris) by integrating a combinatorial peptide ligand library approach with FT-ICR MS

Toxicon. 2015 Aug:102:81-8. doi: 10.1016/j.toxicon.2013.10.002. Epub 2015 Jun 10.

Abstract

Within the Apidae, the largest family of bees with over 5600 described species, the honeybee is the sole species with a well studied venom proteome. So far, only little research has focused on bumblebee venom. Recently, the genome sequence of the European large earth bumblebee (Bombus terrestris) became available and this allowed the first in-depth proteomic analysis of its venom composition. We identified 57 compounds, with 52 of them never described in bumblebee venom. Remarkably, 72% of the detected compounds were found to have a honeybee venom homolog, which reflects the similar defensive function of both venoms and the high degree of homology between both genomes. However, both venoms contain a selection of species-specific toxins, revealing distinct damaging effects that may have evolved in response to species-specific attackers. Further, this study extends the list of potential venom allergens. The availability of both the honeybee and bumblebee venom proteome may help to develop a strategy that solves the current issue of false double sensitivity in allergy diagnosis, which is caused by cross-reactivity between both venoms. A correct diagnosis is important as it is recommended to perform an immunotherapy with venom of the culprit species.

Keywords: Bumblebee; Fourier transform-ion cyclotron resonance mass spectrometry; Hymenoptera; Proteomics; Venom; Venom allergy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bee Venoms / chemistry*
  • Bees*
  • Insect Proteins / analysis*
  • Ligands
  • Peptide Library*
  • Proteome / analysis*
  • Proteomics*
  • Species Specificity

Substances

  • Bee Venoms
  • Insect Proteins
  • Ligands
  • Peptide Library
  • Proteome