| Autor: |
Christiana Vargas Ribeiro, Bruna Fonte Boa Rocha, Douglas de Souza Moreira, Vanessa Peruhype-Magalhães, Silvane Maria Fonseca Murta |
| Jazyk: |
angličtina |
| Rok vydání: |
2019 |
| Předmět: |
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| Zdroj: |
Parasites & Vectors, Vol 12, Iss 1, Pp 1-7 (2019) |
| Druh dokumentu: |
article |
| ISSN: |
1756-3305 |
| DOI: |
10.1186/s13071-019-3305-2 |
| Popis: |
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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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