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Modulation of the Unfolded Protein Response by the Severe Acute Respiratory Syndrome Coronavirus Spike Protein
- Source :
- Journal of Virology
- Publication Year :
- 2006
- Publisher :
- American Society for Microbiology, 2006.
-
Abstract
- Perturbation of the function of endoplasmic reticulum (ER) causes stress leading to the activation of cell signaling pathways known as the unfolded protein response (UPR). Severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) uses ER as a site for synthesis and processing of viral proteins. In this report, we demonstrate that infection with SARS-CoV induces the UPR in cultured cells. A comparison with M, E, and NSP6 proteins indicates that SARS-CoV spike (S) protein sufficiently induces transcriptional activation of several UPR effectors, including glucose-regulated protein 78 (GRP78), GRP94, and C/EBP homologous protein. A substantial amount of S protein accumulates in the ER. The expression of S protein exerts different effects on the three major signaling pathways of the UPR. Particularly, it induces GRP78/94 through PKR-like ER kinase but has no influence on activating transcription factor 6 or X box-binding protein 1. Taken together, our findings suggest that SARS-CoV S protein specifically modulates the UPR to facilitate viral replication.
- Subjects :
- Protein Denaturation
viruses
Immunology
Activating transcription factor
Biology
medicine.disease_cause
Endoplasmic Reticulum
Microbiology
Cell Line
Viral Envelope Proteins
Virology
Heat shock protein
Chlorocebus aethiops
medicine
Animals
Humans
HSP70 Heat-Shock Proteins
Endoplasmic Reticulum Chaperone BiP
Vero Cells
Heat-Shock Proteins
Coronavirus
Membrane Glycoproteins
Ccaat-enhancer-binding proteins
Endoplasmic reticulum
fungi
Membrane Proteins
Molecular biology
Virus-Cell Interactions
Membrane protein
Severe acute respiratory syndrome-related coronavirus
Insect Science
Spike Glycoprotein, Coronavirus
Unfolded protein response
CCAAT-Enhancer-Binding Proteins
Signal transduction
Molecular Chaperones
Plasmids
Subjects
Details
- ISSN :
- 0022538X
- Volume :
- 80
- Issue :
- 18
- Database :
- OpenAIRE
- Journal :
- Journal of Virology
- Accession number :
- edsair.doi.dedup.....55f01efd64f83bb565c23c26b6016268
- Full Text :
- https://doi.org/10.1128/jvi.00659-06