Hymenoptera venom review focusing on Apis mellifera

Abstract

Hymenoptera venoms are complex mixtures containing simple organic molecules, proteins, peptides, and other bioactive elements. Several of these components have been isolated and characterized, and their primary structures determined by biochemical techniques. These compounds are responsible for many toxic or allergic reactions in different organisms, such as local pain, inflammation, itching, irritation, and moderate or severe allergic reactions. The most extensively characterized Hymenoptera venoms are bee venoms, mainly from the Apis genus and also from social wasps and ant species. However, there is little information about other Hymenoptera groups. The Apis venom presents high molecular weight molecules - enzymes with a molecular weight higher than 10.0 kDa - and peptides. The best studied enzymes are phospholipase A2, responsible for cleaving the membrane phospholipids, hyaluronidase, which degrades the matrix component hyaluronic acid into non-viscous segments and acid phosphatase acting on organic phosphates. The main peptide compounds of bee venom are lytic peptide melittin, apamin (neurotoxic), and mastocyte degranulating peptide (MCD)

Detection of honeybee venom in envenomed tissues by direct MALDI MSI

“…In 2005, Peiren and coworkers reported that VIT with recombinant HBV allergens, assayed in stage I clinical trials, was more specific and safer than treatments employing bee-derived venom [9]. A full venom characterization would also help to possibly improve current HBV based therapeutics, reported in particular for arthritic and rheumatic conditions [12].…”

“…Api m1 is the most characterized honeybee venom allergen and is reported to account for 10% to 12% of crude venom [12]. The primary amino sequence of the mature protein has a MW of ϳ15.2 kDa.…”

“…The allergenic actions of Api m 1 are a result of scavenging actions on biological membranes, disrupting the main conformation and producing lysophospholipids as well as long-chain anionic fatty acids. Many studies have reported a synergistic activity with melittin, where the latter would open membrane channels leading to the exposure of the phospholipid catalytic site of Api m 1 [3,12].…”

“…Although the biological mechanism of action is not fully elucidated, the deduced amino acid sequence for Api m 3 exhibits several features in common with high molecular weight phosphatases, which hydrolyze phosphomonoesters in a two step mechanism involving a histidine at the active site [8]. Api m 4, a basic peptide of 26 residues (ϳ2.8 kDa), is considered a minor allergen and accounts for 45% to 50% of the venom dry weight [12,19]. Api m 4 exhibits an amphipathic structure; its polar and nonpolar ends allow it to interact with lipid membranes and ultimately increases permeability.…”

“…Its neurotoxic action results from blocking the sodium and calcium post-synaptic ion channels and this, in turn, blocks many inhibitory or hyper-polarization effects, including ␣-adrenergic, cholinergic, and purinergic pathways. In neurons of both vertebrates and invertebrates, the post-synaptic ion channels play an important role in repetitive activities, therefore apamine downstream action ultimately blocks these activities [12].…”