Title :

Host glycosylation pathways and the unfolded protein response contribute to the infection by Francisella: Glycosylation and UPR in Francisella

Author(s) :

Barel, Monique [Auteur]
Université Paris Descartes - Paris 5 [UPD5]
Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)]
Harduin Lepers, Anne [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Portier, Lucie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Slomianny, Marie-Christine [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Charbit, Alain [Auteur]
Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)]
Université Paris Descartes - Paris 5 [UPD5]

Journal title :

Cellular microbiology

Volume number :

18

Pages :

1763-1781

Publication date :

2016-12

HAL domain(s) :

Chimie/Chimie théorique et/ou physique

English abstract : [en]

Protein glycosylation processes play a crucial role in most physiological functions, including cell signalling, cellular differentiation and adhesion. We previously demonstrated that rapid deglycosylation of membrane ...
Show more >Protein glycosylation processes play a crucial role in most physiological functions, including cell signalling, cellular differentiation and adhesion. We previously demonstrated that rapid deglycosylation of membrane proteins was specifically triggered after infection of human macrophages by the bacterial pathogen Francisella tularensis. Using a glycan processing gene microarray, we found here that Francisella infection modulated expression of numerous glycosidase and glycosyltransferase genes. Furthermore, analysis of cell extracts from infected macrophages by Lectin and Western blotting revealed an important increase of N‐ and O‐protein glycosylation. We chose to focus in the present work on one of the O‐glycosylated proteins identified by mass spectrometry, the multifunctional endoplasmic reticulum chaperone BiP (HSPA5/GRP78). We demonstrate that BiP expression is modulated upon Francisella infection and is required to support its intracellular multiplication. Moreover, we show that Francisella differentially modulates the BiP‐dependent activation of three key proteins of the unfolded protein response (UPR), IRE1, PERK and ATF6. The effects exerted on human cells by Francisella may thus constitute a novel excample of UPR manipulation contributing to intracellular bacterial adaptation.Show less >

Language :

Anglais

Audience :

Non spécifiée

Administrative institution(s) :

CNRS
Université de Lille

Collections :

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

Research team(s) :

Régulation de la glycosylation terminale

Submission date :

2020-02-12T15:44:41Z
2021-03-05T11:59:29Z
2021-03-05T12:00:52Z
2021-03-05T12:05:32Z
2021-03-05T12:07:23Z