TY - JOUR
T1 - Apart from rhoptries, identification of Toxoplasma gondii's O-GlcNAcylated proteins reinforces the universality of the O-GlcNAcome
AU - Aquino-Gil, Moyira Osny
AU - Kupferschmid, Mattis
AU - Shams-Eldin, Hosam
AU - Schmidt, Jörg
AU - Yamakawa, Nao
AU - Mortuaire, Marlène
AU - Krzewinski, Frédéric
AU - Hardivillé, Stéphan
AU - Zenteno, Edgar
AU - Rolando, Christian
AU - Bray, Fabrice
AU - Campos, Eduardo Pérez
AU - Dubremetz, Jean François
AU - Perez-Cervera, Yobana
AU - Schwarz, Ralph T.
AU - Lefebvre, Tony
N1 - Publisher Copyright:
© 2018 Aquino-Gil, Kupferschmid, Shams-Eldin, Schmidt, Yamakawa, Mortuaire, Krzewinski, Hardivillé, Zenteno, Rolando, Bray, Pérez Campos, Dubremetz, Perez-Cervera, Schwarz and Lefebvre.
PY - 2018/8/20
Y1 - 2018/8/20
N2 - 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.
AB - 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.
KW - O-GlcNAcome
KW - O-GlcNAcylation
KW - Proteomics
KW - Rhoptries
KW - T. gondii
KW - Toxoplasmosis
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U2 - 10.3389/fendo.2018.00450
DO - 10.3389/fendo.2018.00450
M3 - Article
C2 - 30177911
AN - SCOPUS:85052237896
VL - 9
JO - Frontiers in Endocrinology
JF - Frontiers in Endocrinology
SN - 1664-2392
IS - AUG
M1 - 450
ER -