Title :

Apart From Rhoptries, Identification of Toxoplasma gondii's O-GlcNAcylated Proteins Reinforces the Universality of the O-GlcNAcome

Author(s) :

Aquino-Gil, Moyira Osny [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Kupferschmid, Mattis [Auteur]
Shams-Eldin, Hosam [Auteur]
Schmidt, Jörg [Auteur]
Yamakawa, Nao [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Plateforme d’Analyse des Glycoconjugués - PLBS [PAGés]
Mortuaire, marlène [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Krzewinski, Frederic [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Hardivillé, Stéphan [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Zenteno, Edgar [Auteur]
Rolando, Christian [Auteur]
Miniaturisation pour la Synthèse, l’Analyse et la Protéomique - UAR 3290 [MSAP]
Miniaturisation pour la Synthèse, l'Analyse et la Protéomique (MSAP) - USR 3290
Bray, Fabrice [Auteur]
Miniaturisation pour la Synthèse, l’Analyse et la Protéomique - UAR 3290 [MSAP]
Miniaturisation pour la Synthèse, l'Analyse et la Protéomique (MSAP) - USR 3290
Pérez Campos, Eduardo [Auteur]
Dubremetz, Jean-François [Auteur]
Perez-Cervera, Yobana [Auteur]
Schwarz, Ralph T. [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Lefebvre, Tony [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Schwarz, Ralph T. [Auteur]

Journal title :

Frontiers in endocrinology

Volume number :

9

Publication date :

2018-08-20

ISSN :

1664-2392

English keyword(s) :

T. gondii
O-GlcNAcylation
O-GlcNAcome
rhoptries
toxoplasmosis
Proteomics

HAL domain(s) :

Chimie/Chimie théorique et/ou physique

English abstract : [en]

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 ...
Show more >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.Show less >

Language :

Anglais

Audience :

Internationale

Popular science :

Non

Administrative institution(s) :

CNRS
Université de Lille

Collections :

• Miniaturisation pour la Synthèse, l'Analyse et la Protéomique (MSAP) - USR 3290
• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Research team(s) :

O-GlcNAcylation, signalisation cellulaire et cycle cellulaire

Submission date :

2020-02-12T15:45:30Z
2021-05-18T07:56:26Z
2024-03-14T09:35:36Z