Author | Santos, André L. S. | |
Author | d`Avila-Levy, Claudia M. | |
Author | Elias, Camila G. R. | |
Author | Vermelho, Alane B. | |
Author | Branquinha, Marta H. | |
Access date | 2020-02-06T16:51:51Z | |
Available date | 2020-02-06T16:51:51Z | |
Document date | 2007 | |
Citation | SANTOS, André L. S. et al. Phytomonas serpens: immunological similarities with the human trypanosomatid pathogens. Microbes and Infection, v. 9, p. 915-921, 2007. | pt_BR |
ISSN | 1286-4579 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/39786 | |
Language | eng | pt_BR |
Publisher | Elsevier | pt_BR |
Rights | restricted access | pt_BR |
Subject in Portuguese | Phytomonas serpens | pt_BR |
Subject in Portuguese | Trypanosomatid | pt_BR |
Subject in Portuguese | Peptidase | pt_BR |
Subject in Portuguese | Trypanosoma cruzi | pt_BR |
Subject in Portuguese | Leishmania spp | pt_BR |
Subject in Portuguese | Immunological similarities | pt_BR |
Subject in Portuguese | Leishmanolysin | pt_BR |
Subject in Portuguese | Cruzipain | pt_BR |
Title | Phytomonas serpens: immunological similarities with the human trypanosomatid pathogens | pt_BR |
Type | Article | pt_BR |
DOI | 10.1016/j.micinf.2007.03.018 | |
Abstract | The present review provides an overview of recent discoveries concerning the immunological similarities between Phytomonas serpens, a tomato
parasite, and human trypanosomatid pathogens, with special emphasis on peptidases. Leishmania spp. and Trypanosoma cruzi express peptidases
that are well-known virulence factors, named leishmanolysin and cruzipain. P. serpens synthesizes two distinct classes of proteolytic
enzymes, metallo- and cysteine-type peptidases, that share common epitopes with leishmanolysin and cruzipain, respectively. The leishmanolysin-
like and cruzipain-like molecules from P. serpens participate in several biological processes including cellular growth and adhesion to the
salivary glands of Oncopeltus fasciatus, a phytophagous insect experimental model. Since previous reports demonstrated that immunization of
mice with P. serpens induced a partial protective immune response against T. cruzi, this plant trypanosomatid may be a suitable candidate for
vaccine studies. Moreover, comparative approaches in the Trypanosomatidae family may be useful to understand kinetoplastid biology, biochemistry
and evolution. | 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. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Bioquímica e Biologia Molecular. 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. 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. 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. Rio de Janeiro, RJ, Brasil. | pt_BR |
Subject | Phytomonas serpens | pt_BR |
Subject | Trypanosoma cruzi | pt_BR |
Subject | Leishmania spp | pt_BR |
Subject | Peptidase | pt_BR |
Subject | Leishmanolisina | pt_BR |
e-ISSN | 1769-714X | |
Embargo date | 2025-01-01 | |