SrasV1, PubMed, Checkpoint, bibRecord, 000A54

The Severe Acute Respiratory Syndrome Coronavirus Nucleocapsid Inhibits Type I Interferon Production by Interfering with TRIM25-Mediated RIG-I Ubiquitination.

Identifieur interne : 000A54 ( PubMed/Checkpoint ); précédent : 000A53; suivant : 000A55

The Severe Acute Respiratory Syndrome Coronavirus Nucleocapsid Inhibits Type I Interferon Production by Interfering with TRIM25-Mediated RIG-I Ubiquitination.

Auteurs : Yong Hu [République populaire de Chine] ; Wei Li [République populaire de Chine] ; Ting Gao [République populaire de Chine] ; Yan Cui [République populaire de Chine] ; Yanwen Jin [République populaire de Chine] ; Ping Li [République populaire de Chine] ; Qingjun Ma [République populaire de Chine] ; Xuan Liu [Oman] ; Cheng Cao [Oman]

Source :

Journal of virology [ 1098-5514 ] ; 2017.

RBID : pubmed:28148787

Descripteurs français

KwdFr :
- Animaux, Facteurs de transcription (métabolisme), Humains, Interféron de type I (métabolisme), Liaison aux protéines, Lignée cellulaire, Protéines nucléocapside (métabolisme), Protéines à motif tripartite (métabolisme), Réplication virale, Tolérance immunitaire, Ubiquitin-protein ligases (métabolisme), Ubiquitinylation, Virus du SRAS (immunologie), Virus du SRAS (pathogénicité), Virus du SRAS (physiologie), Échappement immunitaire.
MESH :
- immunologie : Virus du SRAS.
- métabolisme : Facteurs de transcription, Interféron de type I, Protéines nucléocapside, Protéines à motif tripartite, Ubiquitin-protein ligases.
- pathogénicité : Virus du SRAS.
- physiologie : Virus du SRAS.
- Animaux, Humains, Liaison aux protéines, Lignée cellulaire, Réplication virale, Tolérance immunitaire, Ubiquitinylation, Échappement immunitaire.

English descriptors

KwdEn :
- Animals, Cell Line, Humans, Immune Evasion, Immune Tolerance, Interferon Type I (metabolism), Nucleocapsid Proteins (metabolism), Protein Binding, SARS Virus (immunology), SARS Virus (pathogenicity), SARS Virus (physiology), Transcription Factors (metabolism), Tripartite Motif Proteins (metabolism), Ubiquitin-Protein Ligases (metabolism), Ubiquitination, Virus Replication.
MESH :
- chemical , metabolism : Interferon Type I, Nucleocapsid Proteins, Transcription Factors, Tripartite Motif Proteins, Ubiquitin-Protein Ligases.
- immunology : SARS Virus.
- pathogenicity : SARS Virus.
- physiology : SARS Virus.
- Animals, Cell Line, Humans, Immune Evasion, Immune Tolerance, Protein Binding, Ubiquitination, Virus Replication.

Abstract

Severe acute respiratory syndrome (SARS) is a respiratory disease, caused by a coronavirus (SARS-CoV), that is characterized by atypical pneumonia. The nucleocapsid protein (N protein) of SARS-CoV plays an important role in inhibition of type I interferon (IFN) production via an unknown mechanism. In this study, the SARS-CoV N protein was found to bind to the SPRY domain of the tripartite motif protein 25 (TRIM25) E3 ubiquitin ligase, thereby interfering with the association between TRIM25 and retinoic acid-inducible gene I (RIG-I) and inhibiting TRIM25-mediated RIG-I ubiquitination and activation. Type I IFN production induced by poly I·C or Sendai virus (SeV) was suppressed by the SARS-CoV N protein. SARS-CoV replication was increased by overexpression of the full-length N protein but not N amino acids 1 to 361, which could not interact with TRIM25. These findings provide an insightful interpretation of the SARS-CoV-mediated host innate immune suppression caused by the N protein.IMPORTANCE The SARS-CoV N protein is essential for the viral life cycle and plays a key role in the virus-host interaction. We demonstrated that the interaction between the C terminus of the N protein and the SPRY domain of TRIM25 inhibited TRIM25-mediated RIG-I ubiquitination, which resulted in the inhibition of IFN production. We also found that the Middle East respiratory syndrome CoV (MERS-CoV) N protein interacted with TRIM25 and inhibited RIG-I signaling. The outcomes of these findings indicate the function of the coronavirus N protein in modulating the host's initial innate immune response.

DOI: 10.1128/JVI.02143-16
PubMed: 28148787

Affiliations:

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<term>Tripartite Motif Proteins</term>
<term>Ubiquitin-Protein Ligases</term>
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<term>Protéines à motif tripartite</term>
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) is a respiratory disease, caused by a coronavirus (SARS-CoV), that is characterized by atypical pneumonia. The nucleocapsid protein (N protein) of SARS-CoV plays an important role in inhibition of type I interferon (IFN) production via an unknown mechanism. In this study, the SARS-CoV N protein was found to bind to the SPRY domain of the tripartite motif protein 25 (TRIM25) E3 ubiquitin ligase, thereby interfering with the association between TRIM25 and retinoic acid-inducible gene I (RIG-I) and inhibiting TRIM25-mediated RIG-I ubiquitination and activation. Type I IFN production induced by poly I·C or Sendai virus (SeV) was suppressed by the SARS-CoV N protein. SARS-CoV replication was increased by overexpression of the full-length N protein but not N amino acids 1 to 361, which could not interact with TRIM25. These findings provide an insightful interpretation of the SARS-CoV-mediated host innate immune suppression caused by the N protein.<b>IMPORTANCE</b>
 The SARS-CoV N protein is essential for the viral life cycle and plays a key role in the virus-host interaction. We demonstrated that the interaction between the C terminus of the N protein and the SPRY domain of TRIM25 inhibited TRIM25-mediated RIG-I ubiquitination, which resulted in the inhibition of IFN production. We also found that the Middle East respiratory syndrome CoV (MERS-CoV) N protein interacted with TRIM25 and inhibited RIG-I signaling. The outcomes of these findings indicate the function of the coronavirus N protein in modulating the host's initial innate immune response.</div>
</front>
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<Abstract><AbstractText>Severe acute respiratory syndrome (SARS) is a respiratory disease, caused by a coronavirus (SARS-CoV), that is characterized by atypical pneumonia. The nucleocapsid protein (N protein) of SARS-CoV plays an important role in inhibition of type I interferon (IFN) production via an unknown mechanism. In this study, the SARS-CoV N protein was found to bind to the SPRY domain of the tripartite motif protein 25 (TRIM25) E3 ubiquitin ligase, thereby interfering with the association between TRIM25 and retinoic acid-inducible gene I (RIG-I) and inhibiting TRIM25-mediated RIG-I ubiquitination and activation. Type I IFN production induced by poly I·C or Sendai virus (SeV) was suppressed by the SARS-CoV N protein. SARS-CoV replication was increased by overexpression of the full-length N protein but not N amino acids 1 to 361, which could not interact with TRIM25. These findings provide an insightful interpretation of the SARS-CoV-mediated host innate immune suppression caused by the N protein.<b>IMPORTANCE</b>
 The SARS-CoV N protein is essential for the viral life cycle and plays a key role in the virus-host interaction. We demonstrated that the interaction between the C terminus of the N protein and the SPRY domain of TRIM25 inhibited TRIM25-mediated RIG-I ubiquitination, which resulted in the inhibition of IFN production. We also found that the Middle East respiratory syndrome CoV (MERS-CoV) N protein interacted with TRIM25 and inhibited RIG-I signaling. The outcomes of these findings indicate the function of the coronavirus N protein in modulating the host's initial innate immune response.</AbstractText>
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The Severe Acute Respiratory Syndrome Coronavirus Nucleocapsid Inhibits Type I Interferon Production by Interfering with TRIM25-Mediated RIG-I Ubiquitination.

The Severe Acute Respiratory Syndrome Coronavirus Nucleocapsid Inhibits Type I Interferon Production by Interfering with TRIM25-Mediated RIG-I Ubiquitination.

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