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dc.contributor.authorSilva, Camila Lasse-
dc.contributor.authorAzevedo, Clênia Santos-
dc.contributor.authorAraújo, Carla Nunes de-
dc.contributor.authorMotta, Flávia Nader da Silva-
dc.contributor.authorAndrade, Milene Aparecida-
dc.contributor.authorRocha, Amanda Pereira-
dc.contributor.authorSampaio, Iracyara-
dc.contributor.authorCharneau, Sébastien-
dc.contributor.authorGèze, Marc-
dc.contributor.authorGrellier, Phillippe-
dc.contributor.authorSantana, Jaime Martins de-
dc.contributor.authorBastos, Izabela Marques Dourado-
dc.date.accessioned2024-02-29T13:55:54Z-
dc.date.available2024-02-29T13:55:54Z-
dc.date.issued2020-
dc.identifier.citationLASSE, CAMILA et al. Prolyl oligopeptidase from Leishmania infantum: biochemical characterization and involvement in macrophage infection. Frontiers in Microbiology, [S. l.], v. 11, 2020. DOI: https://doi.org/10.3389/fmicb.2020.01060. Disponível em: https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2020.01060/full.pt_BR
dc.identifier.urihttp://repositorio2.unb.br/jspui/handle/10482/47962-
dc.language.isoengpt_BR
dc.publisherFrontierspt_BR
dc.rightsAcesso Abertopt_BR
dc.titleProlyl oligopeptidase from Leishmania infantum : biochemical characterization and involvement in macrophage infectionpt_BR
dc.typeTrabalho apresentado em eventopt_BR
dc.subject.keywordLeishmania infantumpt_BR
dc.subject.keywordProlil oligopetidasept_BR
dc.identifier.doihttps://doi.org/10.3389/fmicb.2020.01060pt_BR
dc.description.abstract1Leishmania infantum is a flagellated protozoan and one of the main causative agents of visceral leishmaniasis. This disease usually affects the human reticuloendothelial system, can cause death and available therapies may lead to serious side effects. Since it is a neglected tropical disease, the incentives for the development of new drugs are insufficient. It is important to know Leishmania virulence factors that contribute most to the disease in order to develop drugs. In the present work, we have produced L. infantum prolyl oligopeptidase (rPOPLi) in Escherichia coli, and investigated its biochemical properties as well as the effect of POP inhibitors on its enzymatic activity and on the inhibition of the macrophage infection by L. infantum. The optimal activity occurred at pH 7.5 and 37°C in the presence of DTT, the latter increased rPOPLi catalytic efficiency 5-fold on the substrate N-Suc-Gly-Pro-Leu-Gly-Pro-AMC. The enzyme was inhibited by TPCK, TLCK and by two POP specific inhibitors, Z-Pro-prolinal (ZPP, IC50 4.2 nM) and S17092 (IC50 3.5 nM). Besides being a cytoplasmic enzyme, POPLi is also found in punctuate structures within the parasite cytoplasm or associated with the parasite plasma membrane in amastigotes and promastigotes, respectively. Interestingly, S17092 and ZPP prevented parasite invasion in murine macrophages, supporting the involvement of POPLi in the invasive process of L. infantum. These data suggest POPLi as a virulence factor that offers potential as a target for designing new antileishmanial drugs.pt_BR
dc.contributor.affiliationUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratorypt_BR
dc.contributor.affiliationUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratorypt_BR
dc.contributor.affiliationUMR 7245 MCAM, Musèum National d’Histoire Naturelle, Centre National de la Recherche Scientifique, Paris, Francept_BR
dc.contributor.affiliationUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratorypt_BR
dc.contributor.affiliationUniversity of Brasília, Faculty of Ceilandiapt_BR
dc.contributor.affiliationUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratorypt_BR
dc.contributor.affiliationUniversity of Brasília, Faculty of Ceilandiapt_BR
dc.contributor.affiliationUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratorypt_BR
dc.contributor.affiliationUMR 7245 MCAM, Musèum National d’Histoire Naturelle, Centre National de la Recherche Scientifique, Paris, Francept_BR
dc.contributor.affiliationUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratorypt_BR
dc.contributor.affiliationUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratorypt_BR
dc.contributor.affiliationUniversity of Brasília, Department of Cell Biology, Laboratory of Protein Chemistry and Biochemistrypt_BR
dc.contributor.affiliationUMR 7245 MCAM, Musèum National d’Histoire Naturelle, Centre National de la Recherche Scientifique, Paris, Francept_BR
dc.contributor.affiliationCeMIM, Musèum National d’Histoire Naturelle, Paris, Francept_BR
dc.contributor.affiliationUMR 7245 MCAM, Musèum National d’Histoire Naturelle, Centre National de la Recherche Scientifique, Paris, Francept_BR
dc.contributor.affiliationUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratorypt_BR
dc.contributor.affiliationUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratorypt_BR
dc.description.unidadeInstituto de Ciências Biológicas (IB)pt_BR
dc.description.unidadeDepartamento de Biologia Celular (IB CEL)pt_BR
dc.description.unidadeFaculdade UnB Ceilândia (FCE)pt_BR
dc.description.unidadeColegiado de Bases Biológicas e da Saúde (FCE-BASES)pt_BR
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