Titre :

Identification of O-GlcNAcylated proteins in Plasmodium falciparum

Auteur(s) :

Kupferschmid, Mattis [Auteur]
Institut für Virologie
Philipps Universität Marburg = Philipps University of Marburg
Aquino-Gil, Moyira Osny [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Universidad Nacional Autónoma de México = National Autonomous University of Mexico [UNAM]
Shams-Eldin, Hosam [Auteur]
Institut für Virologie
Philipps Universität Marburg = Philipps University of Marburg
Schmidt, Jörg [Auteur]
Institut für Virologie
Philipps Universität Marburg = Philipps University of Marburg
Yamakawa, Nao [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Krzewinski, Frederic [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Schwarz, Ralph T. [Auteur]
Institut für Virologie
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Philipps Universität Marburg = Philipps University of Marburg
Lefebvre, Tony [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]

Titre de la revue :

Malaria Journal

Numéro :

16

Date de publication :

2017-12

ISSN :

1475-2875

Mot(s)-clé(s) en anglais :

Plasmodium falciparum
O‑GlcNAcylation
Proteomics
α‑Tubulin
Hsp70
Glycolysis

Discipline(s) HAL :

Chimie/Chimie théorique et/ou physique

Résumé en anglais : [en]

Background: Post‑translational modifications (PTMs) constitute a huge group of chemical modifications increasing the complexity of the proteomes of living beings. PTMs have been discussed as potential anti‑malarial drug ...
Lire la suite >Background: Post‑translational modifications (PTMs) constitute a huge group of chemical modifications increasing the complexity of the proteomes of living beings. PTMs have been discussed as potential anti‑malarial drug targets due to their involvement in many cell processes. O‑GlcNAcylation is a widespread PTM found in different organisms including Plasmodium falciparum. The aim of this study was to identify O‑GlcNAcylated proteins of P. falciparum, to learn more about the modification process and to understand its eventual functions in the Apicomplexans. Methods: The P. falciparum strain 3D7 was amplified in erythrocytes and purified. The proteome was checked for O‑GlcNAcylation using different methods. The level of UDP‑GlcNAc, the donor of the sugar moiety for O‑GlcNAcyla‑tion processes, was measured using high‑pH anion exchange chromatography. O‑GlcNAcylated proteins were enriched and purified utilizing either click chemistry labelling or adsorption on succinyl‑wheat germ agglutinin beads. Proteins were then identified by mass‑spectrometry (nano‑LC MS/MS). Results: While low when compared to MRC5 control cells, P. falciparum disposes of its own pool of UDP‑GlcNAc. By using proteomics methods, 13 O‑GlcNAcylated proteins were unambiguously identified (11 by click‑chemistry and 6 by sWGA‑beads enrichment; 4 being identified by the 2 approaches) in late trophozoites. These proteins are all part of pathways, functions and structures important for the parasite survival. By probing clicked‑proteins with specific antibodies, Hsp70 and α‑tubulin were identified as P. falciparum O‑GlcNAc‑bearing proteins. Conclusions: This study is the first report on the identity of P. falciparum O‑GlcNAcylated proteins. While the parasite O‑GlcNAcome seems close to those of other species, the structural differences exhibited by the proteomes provides a glimpse of innovative therapeutic paths to fight malaria. Blocking biosynthesis of UDP‑GlcNAc in the parasites is another promising option to reduce Plasmodium life cycle.Lire moins >

Langue :

Anglais

Audience :

Non spécifiée

Établissement(s) :

CNRS
Université de Lille

Collections :

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

Équipe(s) de recherche :

O-GlcNAcylation, signalisation cellulaire et cycle cellulaire

Date de dépôt :

2020-02-12T15:45:15Z
2021-05-05T08:34:33Z