ArticleScientific reports2016
The disruption of GDP-fucose de novo biosynthesis suggests the presence of a novel fucose-containing glycoconjugate in Plasmodium asexual blood stages.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Compounds targeting GPI biosynthesis orComputational and structural biotechnology journal · 2022Article
- Unveiling the Sugary Secrets ofFrontiers in microbiology · 2021Review
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- ProteinParasitology · 2019Review
- ProteinFrontiers in cellular and infection microbiology · 2019Article
- Antibody responses to α-Gal in African children vary with age and site and are associated with malaria protection.Scientific reports · 2018Article
- The Apicomplexa-specific glucosamine-6-phosphate N-acetyltransferase gene family encodes a key enzyme for glycoconjugate synthesis with potential as therapeutic target.Scientific reports · 2018Article
- Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts.Nature communications · 2017Article
- Genetic metabolic complementation establishes a requirement for GDP-fucose inThe Journal of biological chemistry · 2017Article
- Sugar nucleotide quantification by liquid chromatography tandem mass spectrometry reveals a distinct profile inThe Biochemical journal · 2017Article
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Authors and funding
8 authors at 6 institutions in 3 countries.
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Abstract
Glycosylation is an important posttranslational protein modification in all eukaryotes. Besides glycosylphosphatidylinositol (GPI) anchors and N-glycosylation, O-fucosylation has been recently reported in key sporozoite proteins of the malaria parasite. Previous analyses showed the presence of GDP-fucose (GDP-Fuc), the precursor for all fucosylation reactions, in the blood stages of Plasmodium falciparum. The GDP-Fuc de novo pathway, which requires the action of GDP-mannose 4,6-dehydratase (GMD) and GDP-L-fucose synthase (FS), is conserved in the parasite genome, but the importance of fucose metabolism for the parasite is unknown. To functionally characterize the pathway we generated a PfGMD mutant and analyzed its phenotype. Although the labelling by the fucose-binding Ulex europaeus agglutinin I (UEA-I) was completely abrogated, GDP-Fuc was still detected in the mutant. This unexpected result suggests the presence of an alternative mechanism for maintaining GDP-Fuc in the parasite. Furthermore, PfGMD null mutant exhibited normal growth and invasion rates, revealing that the GDP-Fuc de novo metabolic pathway is not essential for the development in culture of the malaria parasite during the asexual blood stages. Nonetheless, the function of this metabolic route and the GDP-Fuc pool that is generated during this stage may be important for gametocytogenesis and sporogonic development in the mosquito.
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