Prolyl oligopeptidase from Leishmania infantum : biochemical characterization and involvement in macrophage infection

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Autor(es): dc.contributorUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratory-
Autor(es): dc.contributorUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratory-
Autor(es): dc.contributorUMR 7245 MCAM, Musèum National d’Histoire Naturelle, Centre National de la Recherche Scientifique, Paris, France-
Autor(es): dc.contributorUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratory-
Autor(es): dc.contributorUniversity of Brasília, Faculty of Ceilandia-
Autor(es): dc.contributorUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratory-
Autor(es): dc.contributorUniversity of Brasília, Faculty of Ceilandia-
Autor(es): dc.contributorUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratory-
Autor(es): dc.contributorUMR 7245 MCAM, Musèum National d’Histoire Naturelle, Centre National de la Recherche Scientifique, Paris, France-
Autor(es): dc.contributorUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratory-
Autor(es): dc.contributorUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratory-
Autor(es): dc.contributorUniversity of Brasília, Department of Cell Biology, Laboratory of Protein Chemistry and Biochemistry-
Autor(es): dc.contributorUMR 7245 MCAM, Musèum National d’Histoire Naturelle, Centre National de la Recherche Scientifique, Paris, France-
Autor(es): dc.contributorCeMIM, Musèum National d’Histoire Naturelle, Paris, France-
Autor(es): dc.contributorUMR 7245 MCAM, Musèum National d’Histoire Naturelle, Centre National de la Recherche Scientifique, Paris, France-
Autor(es): dc.contributorUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratory-
Autor(es): dc.contributorUniversity of Brasília, Department of Cell Biology, Pathogen-Host Interface Laboratory-
Autor(es): dc.creatorSilva, Camila Lasse-
Autor(es): dc.creatorAzevedo, Clênia Santos-
Autor(es): dc.creatorAraújo, Carla Nunes de-
Autor(es): dc.creatorMotta, Flávia Nader da Silva-
Autor(es): dc.creatorAndrade, Milene Aparecida-
Autor(es): dc.creatorRocha, Amanda Pereira-
Autor(es): dc.creatorSampaio, Iracyara-
Autor(es): dc.creatorCharneau, Sébastien-
Autor(es): dc.creatorGèze, Marc-
Autor(es): dc.creatorGrellier, Phillippe-
Autor(es): dc.creatorSantana, Jaime Martins de-
Autor(es): dc.creatorBastos, Izabela Marques Dourado-
Data de aceite: dc.date.accessioned2025-03-18T19:06:03Z-
Data de disponibilização: dc.date.available2025-03-18T19:06:03Z-
Data de envio: dc.date.issued2024-02-29-
Data de envio: dc.date.issued2024-02-29-
Data de envio: dc.date.issued2019-
Fonte completa do material: dc.identifierhttp://repositorio2.unb.br/jspui/handle/10482/47962-
Fonte completa do material: dc.identifierhttps://doi.org/10.3389/fmicb.2020.01060-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/961386-
Descrição: dc.descriptionLeishmania 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.-
Descrição: dc.descriptionInstituto de Ciências Biológicas (IB)-
Descrição: dc.descriptionDepartamento de Biologia Celular (IB CEL)-
Descrição: dc.descriptionFaculdade de Ciências e Tecnologias em Saúde (FCTS) – Campus UnB Ceilândia-
Descrição: dc.descriptionColegiado de Bases Biológicas e da Saúde (FCTS-BASES)-
Formato: dc.formatapplication/pdf-
Idioma: dc.languageen-
Publicador: dc.publisherFrontiers-
Direitos: dc.rightsAcesso Aberto-
Palavras-chave: dc.subjectLeishmania infantum-
Palavras-chave: dc.subjectProlil oligopetidase-
Título: dc.titleProlyl oligopeptidase from Leishmania infantum : biochemical characterization and involvement in macrophage infection-
Aparece nas coleções:Repositório Institucional – UNB - Rep. 1

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