Journal
TOXINS
Volume 13, Issue 4, Pages -Publisher
MDPI
DOI: 10.3390/toxins13040239
Keywords
Bombus ignitus; bumblebee; carboxylesterase; triglyceride; venom
Categories
Funding
- Dong-A University Research Fund
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BivCaE, a carboxylesterase found in bumblebee venom, acts as a lipolytic agent by degrading blood triglycerides, unlike the phospholipase A(2) found in bee venom, BivCaE does not affect mammalian cells.
Bee venom is a complex mixture composed of peptides, proteins with enzymatic properties, and low-molecular-weight compounds. Although the carboxylesterase in bee venom has been identified as an allergen, the enzyme's role as a venom component has not been previously elucidated. Here, we show the lipolytic activity of a bumblebee (Bombus ignitus) venom carboxylesterase (BivCaE). The presence of BivCaE in the venom secreted by B. ignitus worker bees was confirmed using an anti-BivCaE antibody raised against a recombinant BivCaE protein produced in baculovirus-infected insect cells. The enzymatic activity of the recombinant BivCaE protein was optimal at 40 degrees C and pH 8.5. Recombinant BivCaE protein degrades triglycerides and exhibits high lipolytic activity toward long-chain triglycerides, defining the role of BivCaE as a lipolytic agent. Bee venom phospholipase A(2) binds to mammalian cells and induces apoptosis, whereas BivCaE does not affect mammalian cells. Collectively, our data demonstrate that BivCaE functions as a lipolytic agent in bee venom, suggesting that BivCaE will be involved in distributing the venom via degradation of blood triglycerides.
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