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5th International Conference on Parasitology & Microbiology

Paris, France

Moyira Osny Aquino Gil

Moyira Osny Aquino Gil

University of Sciences and Technologies of Lille, France

Title: The Identification of Toxoplasma Gondii and Plasmodium Falciparum O-Glcnacylated proteins reinforces the universality of the O-Glcnacome

Biography

Biography: Moyira Osny Aquino Gil

Abstract

Toxoplasma gondii is one of the parasites with the highest infection rate worldwide (one third of the world population), mainly threatening primo-infected pregnant women, infants and immunocompromised patients. On the other hand, malaria tropica caused by Plasmodium falciparum is still one of the main causes of death worldwide with major incidence in tropical and subtropical regions. It has been recently described that the dynamic post-translational modification O-GlcNAcylation occurs in both parasites. O-GlcNAcylation is nutrient-dependent and consists in the addition of a single N-acetylglucosamine (GlcNAc) moiety onto serine and threonine residues of cytosolic, nuclear and mitochondrial proteins and is regulated by a couple of enzymes, O-GlcNAc-transferase (OGT), which catalyzes the addition of GlcNAc and O-GlcNAcase (OGA) which removes GlcNAc. The functions managed by O-GlcNAcylation are diverse and include regulation of transcription, replication, protein’s fate, trafficking and signaling. Numerous studies have explored the O-GlcNAcome in a wide variety of biological models but very few focused on protists. In the present work, we used enrichment on sWGA-beads and/or immunopurification to identify O-GlcNAcylated proteins in Toxoplasma gondii and Plasmodium falciparum. Many of the proteins found to be O-GlcNAcylated are originally described in higher eukaryotes and participate in cell shape organization, response to stress, glycolysis, protein synthesis and metabolism. Together, these data show that regardless of proteins strictly specific to organisms, the O-GlcNAcylated proteins are rather similar among living beings