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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Comprehensive Analysis and Biological Characterization of Venom Components from Solitary Scoliid Wasp Campsomeriella annulata annulata

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Alberto-Silva, Carlos [1] ; Vieira Portaro, Fernanda Calheta [2] ; Kodama, Roberto Tadashi [2] ; Pantaleao, Halyne Queiroz [1] ; Inagaki, Hidetoshi [3] ; Nihei, Ken-ichi [4] ; Konno, Katsuhiro [5]
Total Authors: 7
[1] Fed Univ ABC UFABC, Nat & Humanities Sci Ctr, Expt Morphophysiol Lab, BR-09606070 Sao Bernardo Do Campo, SP - Brazil
[2] Butantan Inst, Struct & Funct Biomol Lab, BR-05503900 Sao Paulo, SP - Brazil
[3] Natl Inst Adv Ind Sci & Technol, Biomed Res Inst, 1-1-1 Higashi, Tsukuba, Ibaraki 3058566 - Japan
[4] Utsunomiya Univ, Sch Agr, Utsunomiya, Tochigi 3218505 - Japan
[5] Toyama Univ, Inst Nat Med, Toyama, Toyama 9300194 - Japan
Total Affiliations: 5
Document type: Journal article
Source: TOXINS; v. 13, n. 12 DEC 2021.
Web of Science Citations: 0

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. (AU)

FAPESP's process: 19/20832-7 - Study of the proteases and peptides present in the Tityus serrulatus scorpion venom: deepening knowledge on the venom and seeking for new therapies aimed at treating envenomation
Grantee:Fernanda Calheta Vieira Portaro
Support Opportunities: Regular Research Grants
FAPESP's process: 15/13124-5 - Purification and characterization of peptides present in the venom of African snakes: searching for peptidase inhibitor of medical importance
Grantee:Roberto Tadashi Kodama
Support Opportunities: Scholarships in Brazil - Doctorate