SrasV1, PascalFrancis, Checkpoint, bibRecord, 000453

Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein

Identifieur interne : 000453 ( PascalFrancis/Checkpoint ); précédent : 000452; suivant : 000454

Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein

Auteurs : Ching-Ping Chan [Hong Kong] ; Kam-Leung Siu [Hong Kong] ; King-Tung Chin [Hong Kong] ; Kwok-Yung Yuen [Hong Kong] ; BOJIAN ZHENG [Hong Kong] ; Dong-Yan Jin [Hong Kong]

Source :

Journal of virology [ 0022-538X ] ; 2006.

RBID : Pascal:06-0435751

Descripteurs français

Pascal (Inist)
- Coronavirus, Protéine, Microbiologie, Virologie, Syndrome respiratoire aigu sévère.

English descriptors

KwdEn :
- Coronavirus, Microbiology, Protein, Severe acute respiratory syndrome, Virology.

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.

Affiliations:

Hong Kong

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Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein</title>
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<series><title level="j" type="main">Journal of virology</title>
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<front><div type="abstract" xml:lang="en">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.</div>
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Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein

Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein

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Descripteurs français

English descriptors

Abstract

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