ArticleParasites & vectors2019
Mannosyltransferase (GPI-14) overexpression protects promastigote and amastigote forms of Leishmania braziliensis against trivalent antimony.
Article in Parasites & vectors, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Leishmania major virulence attenuation in vitro: An old conundrum revisited in the omics era.PLoS neglected tropical diseases · 2026Article
- O-mannosylation of misfolded ER proteins promotes ERAD.The EMBO journal · 2026Article
- Genomic characterization of Leishmania (V.) braziliensis associated with antimony therapeutic failure and variable in vitro tolerance to amphotericin B.Scientific reports · 2025Article
- Glycosylphosphatidylinositol Mannosyltransferase Ⅰ Protects Chinese Giant Salamander,International journal of molecular sciences · 2022Article
- N-glycome and N-glycoproteome of a hematophagous parasitic nematodeComputational and structural biotechnology journal · 2021Article
- Comparative transcriptomic analysis of antimony resistant and susceptible Leishmania infantum lines.Parasites & vectors · 2020Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
backgroundGlycosylphosphatidylinositol 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.
resultsGPI-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 (Sb
conclusionsOur results suggest the involvement of the GPI-14 enzyme in the Sb
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