Journal
TOXINS
Volume 13, Issue 12, Pages -Publisher
MDPI
DOI: 10.3390/toxins13120885
Keywords
solitary scoliid wasp; venom; comprehensive analysis; LC-MS; bradykinin-related peptide; linear alpha-helical peptide
Categories
Funding
- State of Sao Paulo Research Foundation (FAPESP) [2015/13124-5, 2019/20832-7]
- Coordination for the Improvement of Higher Education Personnel (CAPES) [001]
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The study investigated the venom components profile of a solitary scoliid wasp through LC-MS and MS/MS analysis, identifying 138 components including bradykinin-related peptides and linear alpha-helical peptides. Evaluation of the biological activities of two main peptides, alpha-campsomerin and beta-campsomerin, showed that only alpha-campsomerin enhanced cell viability in PC12 neuronal cells. Annulatin exhibited histamine releasing activity and low hemolytic activity, but no antimicrobial activities.
Venoms of solitary wasps are utilized for prey capture (insects and spiders), paralyzing them with a stinger injection to be offered as food for their larvae. Thus, the identification and characterization of the components of solitary wasp venoms can have biotechnological application. In the present study, the venom components profile of a solitary scoliid wasp, Campsomeriella annulata annulata, was investigated through a comprehensive analysis using LC-MS and -MS/MS. Online mass fingerprinting revealed that the venom extract contains 138 components, and MS/MS analysis identified 44 complete sequences of the peptide components. The peptides are broadly divided into two classes: bradykinin-related peptides, and linear alpha-helical peptides. Among the components of the first class, the two main peptides, alpha-campsomerin (PRLRRLTGLSPLR) and beta-campsomerin (PRLRRLTGLSPLRAP), had their biological activities evaluated. Both peptides had no effects on metallopeptidases [human neprilysin (NEP) and angiotensin-converting enzyme (ACE)] and acetylcholinesterase (AChE), and had no cytotoxic effects. Studies with PC12 neuronal cells showed that only alpha-campsomerin was able to enhance cell viability, while beta-campsomerin had no effect. It is noteworthy that the only difference between the primary structures from these peptides is the presence of the AP extension at the C-terminus of beta-campsomerin, compared to alpha-campsomerin. Among the linear alpha-helical peptides, annulatin (ISEALKSIIVG-NH2) was evaluated for its biological activities. Annulatin showed histamine releasing activity from mast cells and low hemolytic activity, but no antimicrobial activities against all microbes tested were observed. Thus, in addition to providing unprecedented information on the whole components, the three peptides selected for the study suggest that molecules present in solitary scoliid wasp venoms may have interesting biological activities.
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