Author | Elias, Camila G. R. | |
Author | Aor, Ana Carolina | |
Author | Valle, Roberta S. | |
Author | d`Avila-Levy, Claudia M. | |
Author | Branquinha, Marta H. | |
Author | Santos, André L. S. | |
Access date | 2019-04-29T11:45:40Z | |
Available date | 2019-04-29T11:45:40Z | |
Document date | 2009 | |
Citation | ELIAS, Camila G. R. et al. Cysteine peptidases fromPhytomonas serpens: biochemical and immunological approaches. FEMS Immunol Med Microbiol., v. 57, p. 247–256, 2009. | pt_BR |
ISSN | 0928-8244 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/32806 | |
Language | eng | pt_BR |
Publisher | Oxford University Press | pt_BR |
Rights | restricted access | |
Subject in Portuguese | Phytomonas serpens | pt_BR |
Subject in Portuguese | Trypanosoma cruzi | pt_BR |
Subject in Portuguese | Cruzipain | pt_BR |
Subject in Portuguese | Sorologia de pacientes chagásicos | pt_BR |
Title | Cysteine peptidases from Phytomonas serpens: biochemical and immunological approaches | pt_BR |
Type | Article | |
DOI | 10.1111/j.1574-695X.2009.00604.x | |
Abstract | Phytomonas serpens, a phytoflagellate trypanosomatid, shares common antigens with Trypanosoma cruzi. In the present work, we compared the hydrolytic capability of cysteine peptidases in both trypanosomatids. Trypanosoma cruzi epimastigotes presented a 10-fold higher efficiency in hydrolyzing the cysteine peptidase substrate Z-Phe-Arg-AMC than P. serpens promastigotes. Moreover, two weak cysteine-type gelatinolytic activities were detected in P. serpens, while a strong 50-kDa cysteine peptidase was observed in T. cruzi. Cysteine peptidase activities were detected at twofold higher levels in the cytoplasmic fraction when compared with the membrane-rich or the content released from P. serpens. The cysteine peptidase secreted by P. serpens cleaved several proteinaceous substrates. Corroborating these findings, the cellular distribution of the cruzipain-like molecules in P. serpens was attested through immunocytochemistry analysis. Gold particles were observed in all cellular compartments, including the cytoplasm, plasma membrane, flagellum, flagellar membrane and flagellar pocket. Interestingly, some gold particles were visualized free in the flagellar pocket, suggesting the release of the cruzipain-like molecule. The antigenic properties of the cruzipain-like molecules of P. serpens were also analyzed. Interestingly, sera from chagasic patients recognized both cellular and extracellular antigens of P. serpens, including the cruzipain-like molecule. These results point to the use of P. serpens antigens, especially the cruzipain-like cysteine-peptidases, as an alternative vaccination approach to T. cruzi infection. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Microbiologia Prof. Paulo de Góes. Departamento de Microbiologia Geral. Laboratório de Estudos Integrados em Bioquímica Microbiana. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Microbiologia Prof. Paulo de Góes. Departamento de Microbiologia Geral. Laboratório de Estudos Integrados em Bioquímica Microbiana. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Microbiologia Prof. Paulo de Góes. Departamento de Microbiologia Geral. Laboratório de Estudos Integrados em Bioquímica Microbiana. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia Molecular e Doenças Endêmicas. Rio de Janeiro, RJ. Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Microbiologia Prof. Paulo de Góes. Departamento de Microbiologia Geral. Laboratório de Bioquímica de Proteases. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Microbiologia Prof. Paulo de Góes. Departamento de Microbiologia Geral. Laboratório de Estudos Integrados em Bioquímica Microbiana. Rio de Janeiro, RJ, Brasil. | pt_BR |
Subject | Phytomonas serpens | pt_BR |
Subject | Trypanosoma cruzi | pt_BR |
Subject | Cruzipain | pt_BR |
Subject | Cysteine peptidases | pt_BR |
Subject | Chagasic patient sera | pt_BR |
e-ISSN | 1574-695X | |
Embargo date | 2022-01-01 | |