Shigella flexneri modulates stress granule composition and inhibits stress granule aggregation.

Details

Serval ID
serval:BIB_55FDBB57162A
Type
Article: article from journal or magazin.
Collection
Publications
Title
Shigella flexneri modulates stress granule composition and inhibits stress granule aggregation.
Journal
Cellular microbiology
Author(s)
Vonaesch P., Campbell-Valois F.X., Dufour A., Sansonetti P.J., Schnupf P.
ISSN
1462-5822 (Electronic)
ISSN-L
1462-5814
Publication state
Published
Issued date
07/2016
Peer-reviewed
Oui
Volume
18
Number
7
Pages
982-997
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Abstract
Invasion and multiplication of the facultative, cytosolic, enteropathogen Shigella flexneri within the colonic epithelial lining leads to an acute inflammatory response, fever and diarrhea. During the inflammatory process, infected cells are subjected to numerous stresses including heat, oxidative stress and genotoxic stress. The evolutionarily conserved pathway of cellular stress management is the formation of stress granules that store translationally inactive cellular mRNAs and interfere with cellular signalling pathways by sequestering signalling components. In this study, we investigated the ability of S. flexneri-infected cells to form stress granules in response to exogenous stresses. We found that S. flexneri infection inhibits movement of the stress granule markers eIF3 and eIF4B into stress granules and prevents the aggregation of G3BP1 and eIF4G-containing stress granules. This inhibition occurred only with invasive, but not with non-invasive bacteria and occurred in response to stresses that induce translational arrest through the phosphorylation of eIF2α and by treating cells with pateamine A, a drug that induces stress granules by inhibiting the eIF4A helicase. The S. flexneri-mediated stress granule inhibition could be largely phenocopied by the microtubule-destabilizing drug nocodazole and while S. flexneri infection did not lead to microtubule depolymerization, infection greatly enhanced acetylation of alpha-tubulin. Our data suggest that qualitative differences in the microtubule network or subversion of the microtubule-transport machinery by S. flexneri may be involved in preventing the full execution of this cellular stress response.
Keywords
Actins/metabolism, Carrier Proteins/metabolism, Cytoplasmic Granules/metabolism, DNA Helicases, Dysentery, Bacillary/metabolism, Dysentery, Bacillary/microbiology, Dysentery, Bacillary/pathology, Epoxy Compounds/pharmacology, Eukaryotic Initiation Factor-2/metabolism, Eukaryotic Initiation Factor-3/metabolism, Eukaryotic Initiation Factors/metabolism, Golgi Apparatus/metabolism, Golgi Apparatus/microbiology, HeLa Cells/microbiology, Host-Pathogen Interactions/drug effects, Host-Pathogen Interactions/physiology, Humans, Macrolides/pharmacology, Microtubules/metabolism, Mutation, Phosphorylation, Poly-ADP-Ribose Binding Proteins, RNA Helicases, RNA Recognition Motif Proteins, Shigella flexneri/drug effects, Shigella flexneri/genetics, Shigella flexneri/pathogenicity, Stress, Physiological/physiology, Thiazoles/pharmacology
Pubmed
Web of science
Open Access
Yes
Create date
12/08/2022 14:26
Last modification date
03/01/2025 15:27
Usage data