Bottom-up proteomic analysis of polypeptide venom components of the giant ant Dinoponera quadriceps

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dc.contributorLaboratório de Bioquímica e Biofísicapt_BR
dc.contributorLaboratório Especial de Toxinologia Aplicada (LETA)pt_BR
dc.contributorLaboratório de Genéticapt_BR
dc.contributor.authorMariano, Douglas Oscar Ceolinpt_BR
dc.contributor.authorOliveira, Ursula Castro dept_BR
dc.contributor.authorZaharenko, Andre Junqueirapt_BR
dc.contributor.authorPimenta, Daniel Carvalhopt_BR
dc.contributor.authorRadis-Baptista, Gandhipt_BR
dc.contributor.authorPrieto da Silva, Álvaro Rossan de Brandãopt_BR
dc.date.accessioned2020-07-09T21:25:03Z-
dc.date.available2020-07-09T21:25:03Z-
dc.date.issued2019-
dc.identifier.citationMariano DOC, Oliveira UC, Zaharenko AJ, Pimenta DC, Radis-Baptista G, Prieto da Silva ARB. Bottom-up proteomic analysis of polypeptide venom components of the giant ant Dinoponera quadriceps. Toxins. 2019 Jul;11(8):448. doi:10.3390/toxins11080448.pt_BR
dc.identifier.issn2072-6651-
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2829-
dc.description.abstractnt species have specialized venom systems developed to sting and inoculate a biological cocktail of organic compounds, including peptide and polypeptide toxins, for the purpose of predation and defense. The genus Dinoponera comprises predatory giant ants that inoculate venom capable of causing long-lasting local pain, involuntary shaking, lymphadenopathy, and cardiac arrhythmias, among other symptoms. To deepen our knowledge about venom composition with regard to protein toxins and their roles in the chemical–ecological relationship and human health, we performed a bottom-up proteomics analysis of the crude venom of the giant ant D. quadriceps, popularly known as the "false" tocandiras. For this purpose, we used two different analytical approaches: (i) gel-based proteomics approach, wherein the crude venom was resolved by denaturing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and all protein bands were excised for analysis; (ii) solution-based proteomics approach, wherein the crude venom protein components were directly fragmented into tryptic peptides in solution for analysis. The proteomic data that resulted from these two methodologies were compared against a previously annotated transcriptomic database of D. quadriceps, and subsequently, a homology search was performed for all identified transcript products. The gel-based proteomics approach unequivocally identified nine toxins of high molecular mass in the venom, as for example, enzymes [hyaluronidase, phospholipase A1, dipeptidyl peptidase and glucose dehydrogenase/flavin adenine dinucleotide (FAD) quinone] and diverse venom allergens (homologous of the red fire ant Selenopsis invicta) and venom-related proteins (major royal jelly-like). Moreover, the solution-based proteomics revealed and confirmed the presence of several hydrolases, oxidoreductases, proteases, Kunitz-like polypeptides, and the less abundant inhibitor cysteine knot (ICK)-like (knottin) neurotoxins and insect defensin. Our results showed that the major components of the D. quadriceps venom are toxins that are highly likely to damage cell membranes and tissue, to cause neurotoxicity, and to induce allergic reactions, thus, expanding the knowledge about D. quadriceps venom composition and its potential biological effects on prey and victims.pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.format.extent448pt_BR
dc.languageengpt_BR
dc.publisherMDPIpt_BR
dc.relation.ispartofToxinspt_BR
dc.rightsOpen Accesspt_BR
dc.titleBottom-up proteomic analysis of polypeptide venom components of the giant ant Dinoponera quadricepspt_BR
dc.typeArticlept_BR
dc.identifier.doi10.3390/toxins11080448pt_BR
dc.identifier.urlhttps://doi.org/10.3390/toxins11080448pt_BR
dc.contributor.externalUniversidade Federal do Ceará (UFC)¦¦Brasilpt_BR
dc.publisher.cityBaselpt_BR
dc.identifier.citationvolume11pt_BR
dc.identifier.citationissue8pt_BR
dc.subject.keywordDinoponera quadricepspt_BR
dc.subject.keywordFormicidaept_BR
dc.subject.keywordHymenoptera venompt_BR
dc.subject.keywordproteomicspt_BR
dc.subject.keywordvenom allergenspt_BR
dc.subject.keywordICK-like toxinspt_BR
dc.relation.ispartofabbreviatedToxinspt_BR
dc.identifier.citationabntv. 11, n. 8, p. 448, jul. 2019pt_BR
dc.identifier.citationvancouver2019 Jul;11(8):448pt_BR
dc.publisher.countrySwitzerlandpt_BR
dc.contributor.butantanMariano, Douglas Oscar Ceolin|:Aluno|:Laboratório de Bioquímica e Biofísica|:PrimeiroAutorpt_BR
dc.contributor.butantanPimenta, Daniel Carvalho|:Pesquisador:Docente Permanente PPGTOX|:Laboratório de Bioquímica e Biofísica|:pt_BR
dc.contributor.butantanOliveira, Ursula Castro de|:Aluno|:Laboratório Especial de Toxinologia Aplicada (LETA)|:pt_BR
dc.contributor.butantanZaharenko, Andre Junqueira|:Aluno|:Laboratório de Genética|:pt_BR
dc.contributor.butantanPrieto da Silva, Álvaro Rossan de Brandão|:Pesquisador|:Laboratório de Genética|:Autor de correspondênciapt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦303792/2016pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦1406385/2018-1pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦307733/2016-5pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦431077/2016-9pt_BR
dc.sponsorship.butantanCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)¦¦pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦13/07467-1pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.subject.researchlineToxinologia estruturalpt_BR
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item.grantfulltextembargo_29990101-
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