Experimental antivenom against serine proteases from the Bothrops jararaca venom obtained in mice, and its comparison with the antibothropic serum from the Butantan Institute

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dc.contributorLaboratório de Imunoquímicapt_BR
dc.contributorLaboratório Especial de Toxinologia Aplicada (LETA)pt_BR
dc.contributor.authorKuniyoshi, Alexandre Kazuopt_BR
dc.contributor.authorKodama, Roberto Tadashipt_BR
dc.contributor.authorCajado-Carvalho, Danielapt_BR
dc.contributor.authorIwai, Leo Keipt_BR
dc.contributor.authorKitano, Eduardo Shigueopt_BR
dc.contributor.authorSilva, Cristiane Castilho Fernandes dapt_BR
dc.contributor.authorDuzzi, Brunopt_BR
dc.contributor.authorSilva, Wilmar Dias dapt_BR
dc.contributor.authorPortaro, Fernanda Calheta Vieirapt_BR
dc.date.accessioned2020-07-09T21:25:08Z-
dc.date.available2020-07-09T21:25:08Z-
dc.date.issued2019-
dc.identifier.citationKuniyoshi AK, Kodama RT, Cajado-Carvalho D, Iwai LK, Kitano ES, Silva CCF, et al. Experimental antivenom against serine proteases from the Bothrops jararaca venom obtained in mice, and its comparison with the antibothropic serum from the Butantan Institute. Toxicon. 2019 Nov;169:59-67. doi:10.1016/j.toxicon.2019.09.001.pt_BR
dc.identifier.issn0041-0101-
dc.identifier.issn1879-3150-
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2835-
dc.description.abstractIn Brazil, snakes from the Bothrops genus are responsible for thousands of accidents, and their venoms are mainly made up of proteolytic enzymes. Although the antibothropic serum produced by the Butantan Institute is remarkable in saving lives, studies show that some symptoms observed in cases of envenoming are not efficiently neutralized. Moreover, our group has shown that the commercial antivenom does not fully neutralize in vitro some serine proteases present in the Bothrops jararaca venom. Therefore, this study focuses on a new method in the production of specific immunoglobulins capable of neutralizing the activities of these enzymes in vitro. For this, a pool of serine proteases that was not inhibited by the commercial antivenom, made up of four enzymes (KN-BJ2, BjSP, HS112 and BPA) from the B. jararaca venom was obtained through two chromatographic steps (DEAE-HPLC and C8-RP-HPLC). The identities of these proteases were confirmed by SDS-PAGE, followed by tryptic digestion and mass spectrometry analysis. This pool was inoculated into BALB/c and C57BL/6 mice, using SBA-15 as adjuvant, and the produced IgGs were purified by affinity chromatography. The sera were characterized by ELISA, avidity and proteolytic neutralization assays. Both animal models responded to the immunization, producing higher IgGs titers when compared to the commercial antivenom. The experimental serum from BALB/c mice presented a better hydrolysis inhibition of the selective fluorescent substrate for serine proteases (~80%) when compared to C57BL/6 (~25%) and the commercial antivenom (<1%) at the dose of 500:1 (weight of antivenom:weight of venom). These results show that a different immunization method using isolated serine proteases improves the toxins neutralizing efficacy and could lead to a better end product to be used as a supplemental medicine to the currently used immunotherapy.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.format.extent59-67pt_BR
dc.languageengpt_BR
dc.publisherPergamon Presspt_BR
dc.relation.ispartofToxiconpt_BR
dc.titleExperimental antivenom against serine proteases from the Bothrops jararaca venom obtained in mice, and its comparison with the antibothropic serum from the Butantan Institutept_BR
dc.typeArticlept_BR
dc.identifier.doi10.1016/j.toxicon.2019.09.001pt_BR
dc.identifier.urlhttps://doi.org/10.1016/j.toxicon.2019.09.001pt_BR
dc.publisher.cityOxfordpt_BR
dc.identifier.citationvolume169pt_BR
dc.subject.keywordBothrops jararacapt_BR
dc.subject.keywordSerine proteasept_BR
dc.subject.keywordVenompt_BR
dc.subject.keywordAntivenompt_BR
dc.relation.ispartofabbreviatedToxiconpt_BR
dc.identifier.citationabntv. 169, p. 59-67, nov. 2019pt_BR
dc.identifier.citationvancouver2019 Nov;169:59-67pt_BR
dc.publisher.countryEnglandpt_BR
dc.contributor.butantanKuniyoshi, Alexandre Kazuo|:Aluno|:Laboratório de Imunoquímica|:PrimeiroAutorpt_BR
dc.contributor.butantanIwai, Leo Kei|:Pesquisador:Docente Colaborador PPGTOX|:Laboratório Especial de Toxinologia Aplicada (LETA)|:pt_BR
dc.contributor.butantanPortaro, Fernanda Calheta Vieira|:Pesquisador:Docente Permanente PPGTOX|:Laboratório de Imunoquímica|:Autor de correspondênciapt_BR
dc.contributor.butantanKodama, Roberto Tadashi|:Aluno|:Laboratório de Imunoquímica|:pt_BR
dc.contributor.butantanCajado-Carvalho, Daniela|:Aluno|:Laboratório de Imunoquímica|:pt_BR
dc.contributor.butantanKitano, Eduardo Shigueo|:Aluno|:Laboratório Especial de Toxinologia Aplicada (LETA)|:pt_BR
dc.contributor.butantanSilva, Cristiane Castilho Fernandes da|:Aluno|:Laboratório de Imunoquímica|:pt_BR
dc.contributor.butantanDuzzi, Bruno|:Aluno|:Laboratório de Imunoquímica|:pt_BR
dc.contributor.butantanSilva, Wilmar Dias da|:Pesquisador|:Laboratório de Imunoquímica|:pt_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)¦¦2015/15364-3pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2013/15344-7pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2015/13124-5pt_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)¦¦2012/06677-00pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.subject.researchlineBioprospecção e desenvolvimentopt_BR
item.fulltextCom Texto completo-
item.grantfulltextembargo_29990101-
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