We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Apart From Rhoptries, Identification of Toxoplasma gondii's O -GlcNAcylated Proteins Reinforces the Universality of the O -GlcNAcome.
- Authors
Aquino-Gil, Moyira Osny; Kupferschmid, Mattis; Shams-Eldin, Hosam; Schmidt, Jörg; Yamakawa, Nao; Mortuaire, Marlène; Krzewinski, Frédéric; Hardivillé, Stéphan; Zenteno, Edgar; Rolando, Christian; Bray, Fabrice; Pérez Campos, Eduardo; Dubremetz, Jean-François; Perez-Cervera, Yobana; Schwarz, Ralph T.; Lefebvre, Tony
- Abstract
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.
- Subjects
TOXOPLASMA gondii; GLUCOSAMINE; POST-translational modification
- Publication
Frontiers in Endocrinology, 2018, pN.PAG
- ISSN
1664-2392
- Publication type
Article
- DOI
10.3389/fendo.2018.00450