{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T01:58:20Z","timestamp":1792807100923,"version":"4.5.0"},"reference-count":53,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2021,12,10]],"date-time":"2021-12-10T00:00:00Z","timestamp":1639094400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"the State of S\u00e3o Paulo Research Foundation (FAPESP)","award":["2015\/13124-5; 2019\/20832-7"],"award-info":[{"award-number":["2015\/13124-5; 2019\/20832-7"]}],"id":[{"id":"https:\/\/ror.org\/02ddkpn78","id-type":"ROR","asserted-by":"crossref"}]},{"name":"the Coordination for the Improvement of Higher Education Personnel (CAPES)","award":["Finance Code 001"],"award-info":[{"award-number":["Finance Code 001"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>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 \u03b1-helical peptides. Among the components of the first class, the two main peptides, \u03b1-campsomerin (PRLRRLTGLSPLR) and \u03b2-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 \u03b1-campsomerin was able to enhance cell viability, while \u03b2-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 \u03b2-campsomerin, compared to \u03b1-campsomerin. Among the linear \u03b1-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.<\/jats:p>","DOI":"10.3390\/toxins13120885","type":"journal-article","created":{"date-parts":[[2021,12,13]],"date-time":"2021-12-13T01:29:33Z","timestamp":1639358973000},"page":"885","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Comprehensive Analysis and Biological Characterization of Venom Components from Solitary Scoliid Wasp Campsomeriella annulata annulata"],"prefix":"10.3390","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4519-8930","authenticated-orcid":false,"given":"Carlos","family":"Alberto-Silva","sequence":"first","affiliation":[{"name":"Experimental Morphophysiology Laboratory, Natural and Humanities Sciences Center, Federal University of ABC (UFABC), S\u00e3o Bernardo do Campo 09606-070, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9582-4699","authenticated-orcid":false,"given":"Fernanda Calheta","family":"Vieira Portaro","sequence":"additional","affiliation":[{"name":"Structure and Functions of Biomolecules Laboratory, Butantan Institute, S\u00e3o Paulo 05503-900, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0565-9018","authenticated-orcid":false,"given":"Roberto Tadashi","family":"Kodama","sequence":"additional","affiliation":[{"name":"Structure and Functions of Biomolecules Laboratory, Butantan Institute, S\u00e3o Paulo 05503-900, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Halyne Queiroz","family":"Pantale\u00e3o","sequence":"additional","affiliation":[{"name":"Experimental Morphophysiology Laboratory, Natural and Humanities Sciences Center, Federal University of ABC (UFABC), S\u00e3o Bernardo do Campo 09606-070, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hidetoshi","family":"Inagaki","sequence":"additional","affiliation":[{"name":"Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba 305-8566, Ibaraki, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ken-ichi","family":"Nihei","sequence":"additional","affiliation":[{"name":"School of Agriculture, Utsunomiya University, Utsunomiya 321-8505, Tochigi, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1949-1845","authenticated-orcid":false,"given":"Katsuhiro","family":"Konno","sequence":"additional","affiliation":[{"name":"Institute of Natural Medicine, University of Toyama, Toyama 930-0194, Toyama, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,12,10]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"R\u00e1dis-Baptista, G., and Konno, K. 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