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

Barkan NP; Bayazit MB; Ozel Demiralp D

doi:10.3390/toxins9110362

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Journal article

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

Barkan NP Department of Biology, Faculty of Science, Hacettepe University, 06800 Ankara, Turkey. pinar.barkan@gu.se.
Bayazit MB Department of Fundamental Neurosciences, University of Lausanne, 1005 Lausanne, Switzerland. mbayazit@unil.ch.
Ozel Demiralp D Faculty of Engineering, Biomedical Engineering, Ankara University, 06830 Ankara, Turkey. ozeldemiralp@gmail.com.

2017-11-16

Published in:

Toxins. - 2017

Electrophoresis, Gel, Two-Dimensional

Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

English 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.

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