Comprehensive analysis and biological characterization of venom components from solitary scoliid wasp Campsomeriella annulata annulata

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dc.contributor(LEFB) Laboratório de Estrutura e Função Biomoléculaspt_BR
dc.contributor.authorAlberto-Silva, Carlospt_BR
dc.contributor.authorPortaro, Fernanda Calheta Vieirapt_BR
dc.contributor.authorKodama, Roberto Tadashipt_BR
dc.contributor.authorPantaleão, Halyne Queirozpt_BR
dc.contributor.authorInagaki, Hidetoshipt_BR
dc.contributor.authorNihei, Ken-ichipt_BR
dc.contributor.authorKonno, Katsuhiropt_BR
dc.date.accessioned2022-01-03T18:59:41Z-
dc.date.available2022-01-03T18:59:41Z-
dc.date.issued2021pt_BR
dc.identifier.citationAlberto-Silva C, Portaro FCV, Kodama RT, Pantaleão HQ, Inagaki H, Nihei K-, et al. Comprehensive analysis and biological characterization of venom components from solitary scoliid wasp Campsomeriella annulata annulata. Toxins. 2021 Dec;13(12):885. doi:10.3390/toxins13120885.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/4067-
dc.description.abstractVenoms 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 α-helical peptides. Among the components of the first class, the two main peptides, α-campsomerin (PRLRRLTGLSPLR) and β-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 α-campsomerin was able to enhance cell viability, while β-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 β-campsomerin, compared to α-campsomerin. Among the linear α-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.pt_BR
dc.description.sponsorship(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulopt_BR
dc.description.sponsorship(CAPES) Coordenação de Aperfeiçoamento de Pessoal de Nível Superiorpt_BR
dc.format.extent885pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofToxinspt_BR
dc.rightsOpen accesspt_BR
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/pt_BR
dc.titleComprehensive analysis and biological characterization of venom components from solitary scoliid wasp Campsomeriella annulata annulatapt_BR
dc.typeArticlept_BR
dc.rights.licenseCC BYpt_BR
dc.identifier.doi10.3390/toxins13120885pt_BR
dc.identifier.urlhttps://doi.org/10.3390/toxins13120885pt_BR
dc.contributor.external(UFABC) Universidade Federal do ABCpt_BR
dc.contributor.external(AIST) National Institute of Advanced Industrial Science and Technologypt_BR
dc.contributor.externalUtsunomiya Universitypt_BR
dc.contributor.externalUniversity of Toyamapt_BR
dc.identifier.citationvolume13pt_BR
dc.identifier.citationissue12pt_BR
dc.subject.keywordsolitary scoliid wasppt_BR
dc.subject.keywordvenompt_BR
dc.subject.keywordcomprehensive analysispt_BR
dc.subject.keywordLC-MSpt_BR
dc.subject.keywordbradykinin-related peptidept_BR
dc.subject.keywordlinear α-helical peptidept_BR
dc.relation.ispartofabbreviatedToxinspt_BR
dc.identifier.citationabntv. 13, n. 12, 885, dez. 2021pt_BR
dc.identifier.citationvancouver2021 Dec;13(12):885pt_BR
dc.contributor.butantanPortaro, Fernanda Calheta Vieira|:Pesquisador:Docente permanente PPGTOX|:Lab. Biologia Estruturalpt_BR
dc.contributor.butantanKodama, Roberto Tadashi|:Desvinculado|:Lab. de Estrutura e Função Biomoléculaspt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦2015/13124-5pt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦2019/20832-7pt_BR
dc.sponsorship.butantan(CAPES) Coordenação de Aperfeiçoamento de Pessoal de Nível Superior¦¦001pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
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item.languageiso639-1English-
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