| Author | Brunoro, Giselle Villa Flor | |
| Author | Caminha, Marcelle Almeida | |
| Author | Ferreira, André Teixeirada da Silva | |
| Author | Leprevost, Felipeda da Veiga | |
| Author | Carvalho, Paulo Costa | |
| Author | Perales, Jonas | |
| Author | Valente, Richard Hemmi | |
| Author | Menna-Barreto, Rubem Figueiredo Sadok | |
| Access date | 2015-04-17T17:04:34Z | |
| Available date | 2015-04-17T17:04:34Z | |
| Document date | 2015 | |
| Citation | BRUNORO, G. V. et al.Reevaluating the Trypanosoma cruzi proteomic map: The shotgun description of bloodstream trypomastigotes. Journal of Proteomics, n.115, p. 58-65, 2015. | pt_BR |
| URI | https://www.arca.fiocruz.br/handle/icict/10076 | |
| Language | eng | pt_BR |
| Publisher | Elsevier | pt_BR |
| Rights | restricted access | |
| Title | Reevaluating the Trypanosoma cruzi proteomic map: The shotgun description of bloodstream trypomastigotes | pt_BR |
| Type | Article | |
| DOI | 10.1016/j.jprot.2014.12.003 | pt_BR |
| Abstract | Chagas disease is a neglected disease, caused by the protozoan Trypanosoma cruzi. This
kinetoplastid presents a cycle involving different forms and hosts, being trypomastigotes
the main infective form. Despite various T. cruzi proteomic studies, the assessment of
bloodstream trypomastigote profile remains unexplored. The aim of this work is T. cruzi
bloodstream form proteomic description. Employing shotgun approach, 17,394 peptides
were identified, corresponding to 7514 proteins of which 5901 belong to T. cruzi. Cytoskeletal
proteins, chaperones, bioenergetics-related enzymes, and trans-sialidases are among the
top-scoring. GO analysis revealed that all T. cruzi compartments were assessed; and
majority of proteins are involved in metabolic processes and/or presented catalytic activity.
The comparative analysis between the bloodstream trypomastigotes and cultured-derived
or metacyclic trypomastigote proteomic profiles pointed to 2202 proteins exclusively
detected in the bloodstream form. These exclusive proteins are related to: (a) surface
proteins; (b) non-classical secretion pathway; (c) cytoskeletal dynamics; (d) cell cycle and
transcription; (e) proteolysis; (f) redoxmetabolism; (g) biosynthetic pathways; (h) bioenergetics;
(i) protein folding; (j) cell signaling; (k) vesicular traffic; (l) DNA repair; and (m) cell death.
This large-scale evaluation of bloodstream trypomastigotes, responsible for the parasite
dissemination in the patient, marks a step forward in the comprehension of Chagas disease
pathogenesis. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | undação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Laboratório de Biologia Celular. Rio de Janeiro, RJ, Brasil | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Carlos Chagas. Laboratório de Proteômica e Engenharia de Proteínas. Paraná, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Carlos Chagas. Laboratório de Proteômica e Engenharia de Proteínas. Paraná, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Subject | Trypanosoma cruzi | pt_BR |
| Subject | Bloodstream trypomastigotes | pt_BR |
| Subject | Proteomics | pt_BR |
| Subject | Mass spectrometry | pt_BR |
| Embargo date | 2016-02 | pt_BR |
