Kn-Ba: a novel serine protease isolated from Bitis arietans snake venom with fibrinogenolytic and kinin-releasing activities

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dc.contributorLab. Imunoquímicapt_BR
dc.contributorLaboratório de Toxinologia Aplicadapt_BR
dc.contributor.authorMegale, Ângela Alice Amadeupt_BR
dc.contributor.authorMagnoli, Fábio Carlospt_BR
dc.contributor.authorKuniyoshi, Alexandre Kazuopt_BR
dc.contributor.authorIwai, Leo Keipt_BR
dc.contributor.authorTambourgi, Denise Vilarinhopt_BR
dc.contributor.authorPortaro, Fernanda Calheta Vieirapt_BR
dc.contributor.authorSilva, Wilmar Dias dapt_BR
dc.date.accessioned2020-07-09T21:22:30Z-
dc.date.available2020-07-09T21:22:30Z-
dc.date.issued2018pt_BR
dc.identifier.citationMegale AAA, Magnoli FC, Kuniyoshi AK, Iwai LK, Tambourgi DV, Portaro FCV, et al. Kn-Ba: a novel serine protease isolated from Bitis arietans snake venom with fibrinogenolytic and kinin-releasing activities. J. Venom. Anim. Toxins Trop. Dis.. 2018 Dec;24:38. doi:10.1186/s40409-018-0176-5.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2645-
dc.description.abstractBackground Bitis arietans is a venomous snake found in sub-Saharan Africa and in parts of Morocco and Saudi Arabia. The envenomation is characterized by local and systemic reactions including pain, blistering, edema and tissue damage, besides hemostatic and cardiovascular disturbances, which can cause death or permanent disabilities in its victims. However, the action mechanisms that provoke these effects remain poorly understood, especially the activities of purified venom components. Therefore, in order to elucidate the molecular mechanisms that make the Bitis arietans venom so potent and harmful to human beings, this study reports the isolation and biochemical characterization of a snake venom serine protease (SVSP). Methods Solubilized venom was fractionated by molecular exclusion chromatography and the proteolytic activity was determined using fluorescent substrates. The peaks that showed serine protease activity were determined by blocking the proteolytic activity with site-directed inhibitors. In sequence, the fraction of interest was submitted to another cycle of molecular exclusion chromatography. The purified serine protease was identified by mass spectrometry and characterized biochemically and immunochemically. Results A serine protease of 33kDa with fibrinogen-degrading and kinin-releasing activities was isolated, described, and designated herein as Kn-Ba. The experimental Butantan Institute antivenom produced against Bitis arietans venom inhibited the Kn-Ba activity. Conclusions The in vitro activities of Kn-Ba can be correlated with the capacity of the venom to provoke bleeding and clotting disorders as well as hypotension, which are common symptoms presented by envenomed victims. Obtaining satisfactory Kn-Ba inhibition through the experimental antivenom is important, given the WHO's recommendation of immunotherapy in cases of human accidents with venomous snakes.pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.description.sponsorshipFundação Butantanpt_BR
dc.format.extent38pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofJournal of Venomous Animals and Toxins Including Tropical Diseasespt_BR
dc.rightsOpen accesspt_BR
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/pt_BR
dc.titleKn-Ba: a novel serine protease isolated from Bitis arietans snake venom with fibrinogenolytic and kinin-releasing activitiespt_BR
dc.typeArticlept_BR
dc.rights.licenseCC BYpt_BR
dc.identifier.doi10.1186/s40409-018-0176-5pt_BR
dc.identifier.urlhttp://dx.doi.org/10.1186/s40409-018-0176-5pt_BR
dc.identifier.citationvolume24pt_BR
dc.subject.keywordBitis arietanspt_BR
dc.subject.keywordVenompt_BR
dc.subject.keywordAntivenompt_BR
dc.subject.keywordSerine proteasept_BR
dc.subject.keywordFibrinogenolyticpt_BR
dc.subject.keywordKinin-releasing activitypt_BR
dc.relation.ispartofabbreviatedJ Venom Anim Toxins Trop Dispt_BR
dc.identifier.citationabntv. 24, 38, dez. 2018pt_BR
dc.identifier.citationvancouver2018 Dec;24:38pt_BR
dc.contributor.butantanMagnoli, Fábio Carlos|:Pesquisador|:Lab. Imunoquímica|:pt_BR
dc.contributor.butantanKuniyoshi, Alexandre Kazuo|:Aluno|:Lab. Imunoquímica|:pt_BR
dc.contributor.butantanSilva, Wilmar Dias da|:Pesquisador|:Lab. Imunoquímica|:pt_BR
dc.contributor.butantanMegale, Ângela Alice Amadeu|:Aluno|:Lab. Imunoquímica|:PrimeiroAutorpt_BR
dc.contributor.butantanIwai, Leo Kei|:Pesquisador:Docente Colaborador PPGTOX|:Laboratório de Toxinologia Aplicada|:pt_BR
dc.contributor.butantanTambourgi, Denise Vilarinho|:Pesquisador:Docente Permanente PPGTOX|:Lab. Imunoquímica|:pt_BR
dc.contributor.butantanPortaro, Fernanda Calheta Vieira|:Pesquisador:Docente Permanente PPGTOX|:Lab. Imunoquímica|:Autor de correspondênciapt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦490048/2005-6pt_BR
dc.sponsorship.butantanCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)¦¦23038.000814/2011-83pt_BR
dc.sponsorship.butantanFundação Butantan¦¦pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2013/07467-1pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2015/15364-3pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦AKK: 2013/15344-7pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦LKI: 2013/07467-1pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
item.languageiso639-1English-
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