Proteome and phosphoproteome of Africanized and European honeybee venoms

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 melittin-the major of its two phosphorylated forms-was less toxic compared to the native peptide.

Venom Composition of Egyptian and Carniolan Honeybee, Apis mellifera L. Affected by Collection Methods.

“…In our study, the band with molecular weights ranging from 97.74 to 133.61 KDa were high molecular weights and might be vitellogenin (Blank et al, 2013;Resende et al, 2013;Li et al, 2013). Vitellogenin categorized as not a putative venom toxin, even though it is proven to be an allergen (Danneels et al, 2015).…”

“…The biochemical composition of HBV toxins has been reported to have triggered immunological, physiological, and neurological responses within victims (Resende et al, 2013). Biologically active substances included in the HBV, are divided into several groups.…”

Profiling the short, linear, non-disulfide bond-containing peptidome from the venom of the scorpion Tityus obscurus

“…A detailed characterization of animal venom based on the profiling of proteomics and peptidomics has been performed using mass spectrometric analysis. The use of LC-MS and MS/MS has been crucial for detection, sequencing, and identification of the rich composition of peptides/proteins from animal venom, contributing to the assignment of the global proteopeptidomic profiles of various Arthropod venoms such as social wasps [11,[26][27][28][29], ants [30], honeybees [31], and spiders [32,33]. The assignment of the proteome complement from scorpion venom has also benefited from the use of mass spectrometric analysis; a detailed analysis of Tityus spp.…”

Production of antibacterial peptide from bee venom via a new strategy for heterologous expression

“…Honey bee venom is a therapeutic modality with a complex mixture of various proteins, peptides and low molecular components, which is widely used in medical treatment for immunity improvement and anti-inflammation [2][3][4]. Bee venom contains several active substances for human beings, such as secapin, which is responsible for imperturbability of mental disorder patients [5]. The characteristics of bee venom have been receiving increasing attention because of their potential use for anticancer drug discovery and development.…”