Design and production of a recombinant hybrid toxin to raise protective antibodies against Loxosceles spider venom

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dc.contributorLab. Imunopatologiapt_BR
dc.contributor.authorCalabria, Paula Andréia Lucaspt_BR
dc.contributor.authorCaetano, Lhiri Hanna De Luccapt_BR
dc.contributor.authorColombini, Mônicapt_BR
dc.contributor.authorMoura-da-Silva, Ana Mariapt_BR
dc.contributor.authorBarbaro, Katia Cristinapt_BR
dc.contributor.authorFaquim Mauro, Eliana Limapt_BR
dc.contributor.authorMagalhães, Geraldo Santanapt_BR
dc.date.accessioned2020-07-09T21:23:18Z-
dc.date.available2020-07-09T21:23:18Z-
dc.date.issued2019pt_BR
dc.identifier.citationCalabria PAL, Falcão LHADLS, Colombini M, Moura-da-Silva AM, Barbaro KC, Faquim Mauro EL, et al. Design and production of a recombinant hybrid toxin to raise protective antibodies against Loxosceles spider venom. Toxins. 2019 Feb;11(2):108. doi:10.3390/toxins11020108.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2699-
dc.description.abstractHuman accidents with spiders of the genus Loxosceles are an important health problem affecting thousands of people worldwide. Patients evolve to severe local injuries and, in many cases, to systemic disturbances as acute renal failure, in which cases antivenoms are considered to be the most effective treatment. However, for antivenom production, the extraction of the venom used in the immunization process is laborious and the yield is very low. Thus, many groups have been exploring the use of recombinant Loxosceles toxins, particularly phospholipases D (PLDs), to produce the antivenom. Nonetheless, some important venom activities are not neutralized by anti-PLD antibodies. Astacin-like metalloproteases (ALMPs) are the second most expressed toxin acting on the extracellular matrix, indicating the importance of its inclusion in the antigen’s formulation to provide a better antivenom. Here we show the construction of a hybrid recombinant immunogen, called LgRec1ALP1, composed of hydrophilic regions of the PLD and the ALMP toxins from Loxosceles gaucho. Although the LgRec1ALP1 was expressed as inclusion bodies, it resulted in good yields and it was effective to produce neutralizing antibodies in mice. The antiserum neutralized fibrinogenolytic, platelet aggregation and dermonecrotic activities elicited by L. gaucho, L. laeta, and L. intermedia venoms, indicating that the hybrid recombinant antigen may be a valuable source for the production of protective antibodies against Loxosceles ssp. venoms. In addition, the hybrid recombinant toxin approach may enrich and expand the alternative antigens for antisera production for other venoms.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.description.sponsorship(CNPq) Conselho Nacional de Desenvolvimento Científico e Tecnológicopt_BR
dc.format.extent108pt_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.titleDesign and production of a recombinant hybrid toxin to raise protective antibodies against Loxosceles spider venompt_BR
dc.typeArticlept_BR
dc.rights.licenseCC BYpt_BR
dc.identifier.doi10.3390/toxins11020108pt_BR
dc.identifier.urlhttp://dx.doi.org/10.3390/toxins11020108pt_BR
dc.identifier.citationvolume11pt_BR
dc.identifier.citationissue2pt_BR
dc.subject.keywordphospholipases Dpt_BR
dc.subject.keywordmetalloproteasespt_BR
dc.subject.keywordLoxosceles spppt_BR
dc.subject.keywordrecombinant toxinspt_BR
dc.subject.keywordhybrid immunogenpt_BR
dc.subject.keywordneutralizing antibodiespt_BR
dc.subject.keywordantivenomspt_BR
dc.relation.ispartofabbreviatedToxinspt_BR
dc.identifier.citationabntv. 11, n. 2, 108, fev. 2019pt_BR
dc.identifier.citationvancouver2019 Feb;11(2):108pt_BR
dc.contributor.butantanCalabria, Paula Andréia Lucas|:Aluno|:Lab. Imunopatologia|:PrimeiroAutorpt_BR
dc.contributor.butantanMagalhães, Geraldo Santana|:Pesquisador:Docente Permanente PPGTOX|:Lab. Imunopatologia|:Autor de correspondênciapt_BR
dc.contributor.butantanDe Lucca, Lhiri Hanna Alves|:Aluno|:Lab. Imunopatologia|:pt_BR
dc.contributor.butantanColombini, Mônica|:Técnico|:Lab. Imunopatologia|:pt_BR
dc.contributor.butantanMoura-da-Silva, Ana Maria|:Docente Permanente PPGTOX|:Lab. Imunopatologia|:pt_BR
dc.contributor.butantanBarbaro, Katia Cristina|:Pesquisador|:Lab. Imunopatologia|:pt_BR
dc.contributor.butantanFaquim-Mauro, Eliana|:Pesquisador|:Lab. Imunopatologia|:pt_BR
dc.sponsorship.butantan(CNPq) Conselho Nacional de Desenvolvimento Científico e Tecnológico¦¦309392/2015-2pt_BR
dc.sponsorship.butantan(CNPq) Conselho Nacional de Desenvolvimento Científico e Tecnológico¦¦304025/2014-3pt_BR
dc.sponsorship.butantan(CAPES) Coordenação de Aperfeiçoamento de Pessoal de Nível Superior¦¦001pt_BR
dc.sponsorship.butantan(CAPES) Coordenação de Aperfeiçoamento de Pessoal de Nível Superior¦¦88887.124146/2014-00 - PROCAD2013pt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦2014/23457-9pt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦2017/1699-8pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.subject.researchlineToxinologia estruturalpt_BR
dc.description.dbindexedYespt_BR
item.grantfulltextopen-
item.languageiso639-1English-
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