Proteomic Characterization of the Venom of Five Bombus (Thoracobombus) Species

Abstract

Venomous animals use venom, a complex biofluid composed of unique mixtures of proteins and peptides, to act on vital systems of the prey or predator. In bees, venom is solely used for defense against predators. However, the venom composition of bumble bees (Bombus sp.) is largely unknown. The Thoracobombus subgenus of Bombus sp. is a diverse subgenus represented by 14 members across Turkey. In this study, we sought out to proteomically characterize the venom of five Thoracobombus species by using bottom-up proteomic techniques. We have obtained two-dimensional polyacrylamide gel (2D-PAGE) images of each species’ venom sample. We have subsequently identified the protein spots by using matrix assisted laser desorption ionization/time-of-flight mass spectrometry (MALDI-TOF MS). We have identified 47 proteins for Bombus humilis, 32 for B. pascuorum, 60 for B. ruderarius, 39 for B. sylvarum, and 35 for B. zonatus. Moreover, we illustrated that intensities of 2DE protein spots corresponding to putative venom toxins vary in a species-specific manner. Our analyses provide the primary proteomic characterization of five bumble bee species’ venom composition.

Venom profile of the European carpenter bee Xylocopa violacea: Evolutionary and applied considerations on its toxin components

“…Most injected venom proteins ( Fig. 3 ) we identified in X. violacea belong to groups shared with honeybees and bumblebees ( Barkan et al, 2017 , 2020 ; Pucca et al, 2019 ). However, it is striking that novel peptide classes are found in the 9 most highly expressed components of the carpenter bee venom, for which activity and function remain to be studied.…”

“…Melittin that was first described in honeybees represents their most dominant venom component and is probably the singular best studied Hymenopteran toxin ( Pucca et al, 2019 ). Melittin-like variants (Bombolitin) are also expressed in venom of Bombus ( Argiolas and Pisano, 1985 ), despite bumblebee venom being dominated by phospholipase A2 in contrast to honeybee venom ( Barkan et al, 2017 , 2020 ; Yoon et al, 2020 ). It was illustrated in recent proteomic studies that most venom components from Apis and Bombus are generally very similar ( Barkan et al, 2017 ; Van Vaerenbergh et al, 2015 ), which is probably linked to the close phylogenetic relationship of these two genera ( Peters et al, 2017 ), see also Fig.…”

Lipolytic Activity of a Carboxylesterase from Bumblebee (Bombus ignitus) Venom

“…Bee venom’s pharmacotherapeutic effects have already been reported in treating several diseases, such as arthritic rheumatism, pain, and neoplastic diseases [ 13 , 14 , 15 ]. Moreover, bee venom proteomic studies have unraveled the venom composition and extended knowledge of potential venom allergens [ 9 , 10 , 18 , 19 ]. Although the bee venom carboxylesterase was identified as an allergen in honeybees and bumblebees [ 9 , 10 ], the enzyme’s functions as a bee venom component are not yet fully understood.…”

“…Various pharmacotherapeutic effects of bee venom have been reported in the treatment of several disorders, including arthritic rheumatism, pain, and cancer [ 13 , 14 , 15 ]. Furthermore, the proteomic analysis of honeybee and bumblebee venoms has unraveled components of bee venom, such as peptides, proteins with enzymatic properties, and low-molecular-weight compounds [ 9 , 10 , 18 , 19 ]. Many studies have determined the biological and pharmacological properties of bee venom components, such as enzymes and peptides [ 9 , 10 , 13 , 20 , 21 , 22 , 23 ].…”

Proteomic and Transcriptomic Techniques to Decipher the Molecular Evolution of Venoms

“…Furthermore, gel electrophoresis can be carried out in native or denaturing conditions depending on the gel used. To carry out electrophoresis of non-denatured (intact) proteins and protein complexes, one can use techniques such as Blue Native-PAGE (BN-PAGE) or Clear Native electrophoresis to separation and isolation of protein complexes (of particular interest in venom studies) [ 55 , 56 ]. With denaturing conditions, such as SDS-PAGE, one can instead separate and isolate denature proteins, in which secondary structures have been broken down.…”