Titre :

Identification of O-Glcnacylated Proteins in Trypanosoma cruzi

Auteur(s) :

Torres-Gutiérrez, Elia [Auteur]
Pérez-Cervera, Yobana [Auteur]
Camoin, Luc [Auteur]
Zenteno, Edgar [Auteur]
Aquino-Gil, Moyira Osny [Auteur]
Lefebvre, Tony [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Cabrera-Bravo, Margarita [Auteur]
Reynoso-Ducoing, Olivia [Auteur]
Bucio-Torres, Martha Irene [Auteur]
Salazar-Schettino, Paz María [Auteur]

Titre de la revue :

Frontiers in Endocrinology

Nom court de la revue :

Front. Endocrinol.

Numéro :

10

Pagination :

199

Éditeur :

Frontiers Media SA

Date de publication :

2019-03-29

ISSN :

1664-2392

Mot(s)-clé(s) en anglais :

Trypanosoma cruzi
O-GlcNAcylated proteins
post translational modification
epimastigote
protist
click chemistry
mass spectrometry

Discipline(s) HAL :

Sciences du Vivant [q-bio]
Chimie/Chimie théorique et/ou physique

Résumé en anglais : [en]

Originally an anthropozoonosis in the Americas, Chagas disease has spread from its previous borders through migration. It is caused by the protozoan Trypanosoma cruzi. Differences in disease severity have been attributed ...
Lire la suite >Originally an anthropozoonosis in the Americas, Chagas disease has spread from its previous borders through migration. It is caused by the protozoan Trypanosoma cruzi. Differences in disease severity have been attributed to a natural pleomorphism in T. cruzi. Several post-translational modifications (PTMs) have been studied in T. cruzi, but to date no work has focused on O-GlcNAcylation, a highly conserved monosaccharide-PTM of serine and threonine residues mainly found in nucleus, cytoplasm, and mitochondrion proteins. O-GlcNAcylation is thought to regulate protein function analogously to protein phosphorylation; indeed, crosstalk between both PTMs allows the cell to regulate its functions in response to nutrient levels and stress. Herein, we demonstrate O-GlcNAcylation in T. cruzi epimastigotes by three methods: by using specific antibodies against the modification in lysates and whole parasites, by click chemistry labeling, and by proteomics. In total, 1,271 putative O-GlcNAcylated proteins and six modification sequences were identified by mass spectrometry (data available via ProteomeXchange, ID PXD010285). Most of these proteins have structural and metabolic functions that are essential for parasite survival and evolution. Furthermore, O-GlcNAcylation pattern variations were observed by antibody detection under glucose deprivation and heat stress conditions, supporting their possible role in the adaptive response. Given the numerous biological processes in which O-GlcNAcylated proteins participate, its identification in T. cruzi proteins opens a new research field in the biology of Trypanosomatids, improve our understanding of infection processes and may allow us to identify new therapeutic targets.Lire moins >

Langue :

Anglais

Comité de lecture :

Oui

Audience :

Internationale

Vulgarisation :

Non

Établissement(s) :

Université de Lille
CNRS

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Équipe(s) de recherche :

O-GlcNAcylation, signalisation cellulaire et cycle cellulaire

Date de dépôt :

2020-12-14T12:57:34Z
2020-12-17T08:42:06Z