ArticleMalaria journal2017
Identification of O-GlcNAcylated proteins in Plasmodium falciparum.
Article in Malaria journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed.
- Article
- Investigation of carbohydrate-based molecules ofFrontiers in veterinary science · 2026Article
- Key Regulators of Parasite Biology Viewed Through a Post-Translational Modification Repertoire.Proteomics · 2025Review
- Hexosamine biosynthesis disruption impairs GPI production and arrests Plasmodium falciparum growth at schizont stages.PLoS pathogens · 2025Article
- The Plasmodium GRASP Homolog Modulates Liver Stage Development, Subsequent Blood Infection and Virulence in Mice.Molecular microbiology · 2025Article
- Post-Translational Modifications of Proteins of Malaria Parasites during the Life Cycle.International journal of molecular sciences · 2024Review
- Glycosylation in malaria parasites: what do we know?Trends in parasitology · 2024Review
- Targeting plasmodium α-tubulin-1 to block malaria transmission to mosquitoes.Frontiers in cellular and infection microbiology · 2023Article
- Beta thalassemia minor is a beneficial determinant of red blood cell storage lesion.Haematologica · 2022Article
- Beyond phosphorylation: Putative roles of post-translational modifications in Plasmodium sexual stages.Molecular and biochemical parasitology · 2021Article
- Mass Spectrometry for O-GlcNAcylation.Frontiers in chemistry · 2021Review
- Unveiling the Sugary Secrets ofFrontiers in microbiology · 2021Review
- Landscapes of Protein Posttranslational Modifications of African Trypanosoma Parasites.iScience · 2020Article
- ProteinParasitology · 2019Review
- High-density Peptide Arrays Help to Identify Linear Immunogenic B-cell Epitopes in Individuals Naturally Exposed to Malaria Infection.Molecular & cellular proteomics : MCP · 2019Article
- Identification ofFrontiers in endocrinology · 2019Article
- Critical observations that shaped our understanding of the function(s) of intracellular glycosylation (O-GlcNAc).FEBS letters · 2018Review
- Plasmodium Parasites Viewed through Proteomics.Trends in parasitology · 2018Review
- Facile Preparation ofMolecules (Basel, Switzerland) · 2018Article
- Apart From Rhoptries, Identification ofFrontiers in endocrinology · 2018Article
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8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundPost-translational modifications (PTMs) constitute a huge group of chemical modifications increasing the complexity of the proteomes of living beings. PTMs have been discussed as potential anti-malarial drug targets due to their involvement in many cell processes. O-GlcNAcylation is a widespread PTM found in different organisms including Plasmodium falciparum. The aim of this study was to identify O-GlcNAcylated proteins of P. falciparum, to learn more about the modification process and to understand its eventual functions in the Apicomplexans.
methodsThe P. falciparum strain 3D7 was amplified in erythrocytes and purified. The proteome was checked for O-GlcNAcylation using different methods. The level of UDP-GlcNAc, the donor of the sugar moiety for O-GlcNAcylation processes, was measured using high-pH anion exchange chromatography. O-GlcNAcylated proteins were enriched and purified utilizing either click chemistry labelling or adsorption on succinyl-wheat germ agglutinin beads. Proteins were then identified by mass-spectrometry (nano-LC MS/MS).
resultsWhile low when compared to MRC5 control cells, P. falciparum disposes of its own pool of UDP-GlcNAc. By using proteomics methods, 13 O-GlcNAcylated proteins were unambiguously identified (11 by click-chemistry and 6 by sWGA-beads enrichment; 4 being identified by the 2 approaches) in late trophozoites. These proteins are all part of pathways, functions and structures important for the parasite survival. By probing clicked-proteins with specific antibodies, Hsp70 and α-tubulin were identified as P. falciparum O-GlcNAc-bearing proteins.
conclusionsThis study is the first report on the identity of P. falciparum O-GlcNAcylated proteins. While the parasite O-GlcNAcome seems close to those of other species, the structural differences exhibited by the proteomes provides a glimpse of innovative therapeutic paths to fight malaria. Blocking biosynthesis of UDP-GlcNAc in the parasites is another promising option to reduce Plasmodium life cycle.
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