Schistosoma mansoni venom allergen-like protein 18 (SmVAL18) is a plasminogen-binding protein secreted during the early stages of mammalian-host infection

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dc.contributorLab. Desenvolvimento de Vacinaspt_BR
dc.contributorLab. Parasitologiapt_BR
dc.contributor.authorFernandes, Rafaela Sachettopt_BR
dc.contributor.authorFernandes, Luis Guilherme Vírgíliopt_BR
dc.contributor.authorde Godoy, Andre S.pt_BR
dc.contributor.authorMiyasato, Patricia Aokipt_BR
dc.contributor.authorNakano, Elianapt_BR
dc.contributor.authorFarias, Leonardo P.pt_BR
dc.contributor.authorNascimento, Ana Lúcia Tabet Oller dopt_BR
dc.contributor.authorLeite, Luciana Cezar de Cerqueirapt_BR
dc.identifier.citationFernandes RS, Fernandes LGV, de Godoy AS., Miyasato PA, Nakano E, Farias LP., et al. Schistosoma mansoni venom allergen-like protein 18 (SmVAL18) is a plasminogen-binding protein secreted during the early stages of mammalian-host infection. Mol. Biochem. Parasitol.. 2018 Apr;221:23-31. doi:10.1016/j.molbiopara.2018.02.003.pt_BR
dc.description.abstractSchistosomiasis is a neglected tropical disease caused by trematodes of the genus Schistosoma which have a complex life cycle characterized by an asexual multiplication phase in the snail intermediate host and a sexual reproduction phase in the mammalian definitive host. The initial steps of the human host infection involve the secretion of proteins contained in the acetabular glands of cercariae that promote parasite adhesion and proteolysis of the skin layers. Herein, we performed a functional analysis of SmVAL18, identified as one of the three SCP/TAPS proteins constituent of cercarial secretions. We evaluated the SmVAL18 binding to immobilized macromolecules of the extracellular matrix (ECM) and to plasma components. Recombinant protein, expressed in E. coli, was found to maintain an ordered secondary structure typical of the SCP/TAPS domain after purification. Expression of native SmVAL18 protein was verified to be restricted to cercariae and 3-h schistosomula stages; furthermore, the protein was observed in the corresponding secretions, confirming that SmVAL18 is secreted during the first 3 h of in vitro culture. rSmVAL18 was able to interact specifically with plasminogen (PLG) and enhance its conversion into plasmin in the presence of the urokinase-type plasminogen activator (uPA). Protein homology modelling suggested that the PLG-rSmVAL18 interaction was mediated by lysine residues of the protein. This was supported by in vitro data using the lysine analogue, 6-aminocaproic acid (ACA), which abolished the interaction. Finally, our results showed that both cercariae and 3-h schistosomula, as well as their corresponding secretions, exhibited the capacity to bind PLG and enhance its conversion into plasmin in vitro in the same way as observed for the recombinant protein. In conclusion, our findings show that SmVAL18 is a novel PLG-binding protein secreted during the early stages of the mammalian-host infection.pt_BR
dc.description.sponsorship(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulopt_BR
dc.format.extentp. 23-31pt_BR
dc.relation.ispartofMolecular and Biochemical Parasitologypt_BR
dc.rightsRestricted accesspt_BR
dc.titleSchistosoma mansoni venom allergen-like protein 18 (SmVAL18) is a plasminogen-binding protein secreted during the early stages of mammalian-host infectionpt_BR
dc.contributor.external(USP) Universidade de São Paulopt_BR
dc.contributor.externalInstituto Gonçalo Moniz (IGM)¦¦Brasilpt_BR
dc.subject.keywordPLG-binding proteinpt_BR
dc.relation.ispartofabbreviatedMol Biochem Parasitolpt_BR
dc.identifier.citationabntv. 221, p. 23-31, abr. 2018pt_BR
dc.identifier.citationvancouver2018 Apr;221:23-31pt_BR
dc.contributor.butantanFernandes, Luis Guilherme Virgílio|:Aluno|:Laboratório de Desenvolvimento de Vacinas|:pt_BR
dc.contributor.butantanMiyasato, Patricia Aoki|:Técnico|:Lab. Parasitologia|:pt_BR
dc.contributor.butantanNakano, Eliana|:Pesquisador|:Lab. Parasitologia|:pt_BR
dc.contributor.butantanNascimento, Ana Lúcia Tabet Oller do|:Pesquisador|:Laboratório de Desenvolvimento de Vacinas|:pt_BR
dc.contributor.butantanLeite, Luciana Cezar de Cerqueira|:Pesquisador|:Laboratório de Desenvolvimento de Vacinas|:Autor de correspondênciapt_BR
dc.contributor.butantanFernandes, Rafaela Sachetto|:Aluno|:Laboratório de Desenvolvimento de Vacinas|:PrimeiroAutorpt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦2012/23124-4pt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦2010/18486-9pt_BR
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