%0 Generic %A Aquino-Gil, Moyira Osny %A Kupferschmid, Mattis %A Shams-Eldin, Hosam %A Schmidt, Jörg %A Yamakawa, Nao %A Mortuaire, Marlène %A Krzewinski, Frédéric %A Hardivillé, Stéphan %A Zenteno, Edgar %A Rolando, Christian %A Bray, Fabrice %A Campos, Eduardo Pérez %A Dubremetz, Jean-François %A Perez-Cervera, Yobana %A Schwarz, Ralph T. %A Lefebvre, Tony %D 2018 %T Table_1_Apart From Rhoptries, Identification of Toxoplasma gondii's O-GlcNAcylated Proteins Reinforces the Universality of the O-GlcNAcome.XLSX %U https://frontiersin.figshare.com/articles/dataset/Table_1_Apart_From_Rhoptries_Identification_of_Toxoplasma_gondii_s_O-GlcNAcylated_Proteins_Reinforces_the_Universality_of_the_O-GlcNAcome_XLSX/6983501 %R 10.3389/fendo.2018.00450.s001 %2 https://frontiersin.figshare.com/ndownloader/files/12808409 %K T. gondii %K O-GlcNAcome %K O-GlcNAcylation %K proteomics %K toxoplasmosis %K rhoptries %X

O-linked β-N-acetylglucosaminylation or O-GlcNAcylation is a widespread post-translational modification that belongs to the large and heterogeneous group of glycosylations. The functions managed by O-GlcNAcylation are diverse and include regulation of transcription, replication, protein's fate, trafficking, and signaling. More and more evidences tend to show that deregulations in the homeostasis of O-GlcNAcylation are involved in the etiology of metabolic diseases, cancers and neuropathologies. O-GlcNAc transferase or OGT is the enzyme that transfers the N-acetylglucosamine residue onto target proteins confined within the cytosolic and nuclear compartments. A form of OGT was predicted for Toxoplasma and recently we were the first to show evidence of O-GlcNAcylation in the apicomplexans Toxoplasma gondii and Plasmodium falciparum. Numerous studies have explored the O-GlcNAcome in a wide variety of biological models but very few focus on protists. In the present work, we used enrichment on sWGA-beads and immunopurification to identify putative O-GlcNAcylated proteins in Toxoplasma gondii. Many of the proteins found to be O-GlcNAcylated were originally described in higher eukaryotes and participate in cell shape organization, response to stress, protein synthesis and metabolism. In a more original way, our proteomic analyses, confirmed by sWGA-enrichment and click-chemistry, revealed that rhoptries, proteins necessary for invasion, are glycosylated. Together, these data show that regardless of proteins strictly specific to organisms, O-GlcNAcylated proteins are rather similar among living beings.

%I Frontiers