Author | Ribeiro, Christiana Vargas | |
Author | Rocha, Bruna Fonte Boa | |
Author | Moreira, Douglas de Souza | |
Author | Pascoal, Vanessa Peruhype Magalhães | |
Author | Murta, Silvane Maria Fonseca | |
Access date | 2019-10-18T17:10:16Z | |
Available date | 2019-10-18T17:10:16Z | |
Document date | 2019 | |
Citation | RIBEIRO, Christiana Vargas et al. Mannosyltransferase (GPI-14) overexpression protects promastigote and amastigote forms of Leishmania braziliensis against trivalent antimony. Parasites & Vectors, v. 12, p. 1-7, 2019. | pt_BR |
ISSN | 1756-3305 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/36577 | |
Language | eng | pt_BR |
Publisher | BioMed Central | pt_BR |
Rights | open access | pt_BR |
Title | Mannosyltransferase (GPI-14) overexpression protects promastigote and amastigote forms of Leishmania braziliensis against trivalent antimony | pt_BR |
Type | Article | pt_BR |
DOI | 10.1371/journal.pone.0211374 | |
Abstract | Background: Glycosylphosphatidylinositol is a surface molecule important for host-parasite interactions. Mannosyltransferase (GPI-14) is an essential enzyme for adding mannose on the glycosylphosphatidyl group. This study attempted to overexpress the GPI-14 gene in Leishmania braziliensis to investigate its role in the antimony-resistance phenotype of this parasite.
Results: GPI-14 mRNA levels determined by quantitative real-time PCR (qRT-PCR) showed an increased expression in clones transfected with GPI-14 compared to its respective wild-type line. In order to investigate the expression profile of the surface carbohydrates of these clones, the intensity of the fluorescence emitted by the parasites after concanavalin-A (a lectin that binds to the terminal regions of α-D-mannosyl and α-D-glucosyl residues) treatment was analyzed. The results showed that the clones transfected with GPI-14 express 2.8-fold more mannose and glucose residues than those of the wild-type parental line, indicating effective GPI-14 overexpression. Antimony susceptibility tests using promastigotes showed that clones overexpressing the GPI-14 enzyme are 2.4- and 10.5-fold more resistant to potassium antimonyl tartrate (SbIII) than the parental non-transfected line. Infection analysis using THP-1 macrophages showed that amastigotes from both GPI-14 overexpressing clones were 3-fold more resistant to SbIII than the wild-type line. Conclusions: Our results suggest the involvement of the GPI-14 enzyme in the SbIII-resistance phenotype of L. braziliensis. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Rene Rachou. Belo Horizonte, MG, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Rene Rachou. Belo Horizonte, MG, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Rene Rachou. Belo Horizonte, MG, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Rene Rachou. Belo Horizonte, MG, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Rene Rachou. Belo Horizonte, MG, Brasil. | pt_BR |
Subject | Leishmania braziliensis | pt_BR |
Subject | Antimony-resistance | pt_BR |
Subject | Leishmanioses | pt_BR |