The cellular RNA helicase DDX1 interacts with coronavirus nonstructural protein 14 and enhances viral replication.
Identifieur interne : 001681 ( PubMed/Corpus ); précédent : 001680; suivant : 001682The cellular RNA helicase DDX1 interacts with coronavirus nonstructural protein 14 and enhances viral replication.
Auteurs : Linghui Xu ; Siti Khadijah ; Shouguo Fang ; Li Wang ; Felicia P L. Tay ; Ding Xiang LiuSource :
- Journal of virology [ 1098-5514 ] ; 2010.
English descriptors
- KwdEn :
- Animals, Cell Nucleus (metabolism), Chlorocebus aethiops, Coronavirus Infections (genetics), Coronavirus Infections (metabolism), Coronavirus Infections (virology), Cytoplasm (metabolism), DEAD-box RNA Helicases (genetics), DEAD-box RNA Helicases (metabolism), HeLa Cells, Humans, Infectious bronchitis virus (genetics), Infectious bronchitis virus (physiology), Protein Binding, Protein Transport, Two-Hybrid System Techniques, Vero Cells, Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism), Virus Replication.
- MESH :
- chemical , genetics : DEAD-box RNA Helicases, Viral Nonstructural Proteins.
- genetics : Coronavirus Infections, Infectious bronchitis virus.
- metabolism : Cell Nucleus, Coronavirus Infections, Cytoplasm, DEAD-box RNA Helicases, Viral Nonstructural Proteins.
- physiology : Infectious bronchitis virus.
- virology : Coronavirus Infections.
- Animals, Chlorocebus aethiops, HeLa Cells, Humans, Protein Binding, Protein Transport, Two-Hybrid System Techniques, Vero Cells, Virus Replication.
Abstract
The involvement of host proteins in the replication and transcription of viral RNA is a poorly understood area for many RNA viruses. For coronaviruses, it was long speculated that replication of the giant RNA genome and transcription of multiple subgenomic mRNA species by a unique discontinuous transcription mechanism may require host cofactors. To search for such cellular proteins, yeast two-hybrid screening was carried out by using the nonstructural protein 14 (nsp14) from the coronavirus infectious bronchitis virus (IBV) as a bait protein, leading to the identification of DDX1, a cellular RNA helicase in the DExD/H helicase family, as a potential interacting partner. This interaction was subsequently confirmed by coimmunoprecipitation assays with cells coexpressing the two proteins and with IBV-infected cells. Furthermore, the endogenous DDX1 protein was found to be relocated from the nucleus to the cytoplasm in IBV-infected cells. In addition to its interaction with IBV nsp14, DDX1 could also interact with the nsp14 protein from severe acute respiratory syndrome coronavirus (SARS-CoV), suggesting that interaction with DDX1 may be a general feature of coronavirus nsp14. The interacting domains were mapped to the C-terminal region of DDX1 containing motifs V and VI and to the N-terminal portion of nsp14. Manipulation of DDX1 expression, either by small interfering RNA-induced knockdown or by overexpression of a mutant DDX1 protein, confirmed that this interaction may enhance IBV replication. This study reveals that DDX1 contributes to efficient coronavirus replication in cell culture.
DOI: 10.1128/JVI.00392-10
PubMed: 20573827
Links to Exploration step
pubmed:20573827Le document en format XML
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<front><div type="abstract" xml:lang="en">The involvement of host proteins in the replication and transcription of viral RNA is a poorly understood area for many RNA viruses. For coronaviruses, it was long speculated that replication of the giant RNA genome and transcription of multiple subgenomic mRNA species by a unique discontinuous transcription mechanism may require host cofactors. To search for such cellular proteins, yeast two-hybrid screening was carried out by using the nonstructural protein 14 (nsp14) from the coronavirus infectious bronchitis virus (IBV) as a bait protein, leading to the identification of DDX1, a cellular RNA helicase in the DExD/H helicase family, as a potential interacting partner. This interaction was subsequently confirmed by coimmunoprecipitation assays with cells coexpressing the two proteins and with IBV-infected cells. Furthermore, the endogenous DDX1 protein was found to be relocated from the nucleus to the cytoplasm in IBV-infected cells. In addition to its interaction with IBV nsp14, DDX1 could also interact with the nsp14 protein from severe acute respiratory syndrome coronavirus (SARS-CoV), suggesting that interaction with DDX1 may be a general feature of coronavirus nsp14. The interacting domains were mapped to the C-terminal region of DDX1 containing motifs V and VI and to the N-terminal portion of nsp14. Manipulation of DDX1 expression, either by small interfering RNA-induced knockdown or by overexpression of a mutant DDX1 protein, confirmed that this interaction may enhance IBV replication. This study reveals that DDX1 contributes to efficient coronavirus replication in cell culture.</div>
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<Abstract><AbstractText>The involvement of host proteins in the replication and transcription of viral RNA is a poorly understood area for many RNA viruses. For coronaviruses, it was long speculated that replication of the giant RNA genome and transcription of multiple subgenomic mRNA species by a unique discontinuous transcription mechanism may require host cofactors. To search for such cellular proteins, yeast two-hybrid screening was carried out by using the nonstructural protein 14 (nsp14) from the coronavirus infectious bronchitis virus (IBV) as a bait protein, leading to the identification of DDX1, a cellular RNA helicase in the DExD/H helicase family, as a potential interacting partner. This interaction was subsequently confirmed by coimmunoprecipitation assays with cells coexpressing the two proteins and with IBV-infected cells. Furthermore, the endogenous DDX1 protein was found to be relocated from the nucleus to the cytoplasm in IBV-infected cells. In addition to its interaction with IBV nsp14, DDX1 could also interact with the nsp14 protein from severe acute respiratory syndrome coronavirus (SARS-CoV), suggesting that interaction with DDX1 may be a general feature of coronavirus nsp14. The interacting domains were mapped to the C-terminal region of DDX1 containing motifs V and VI and to the N-terminal portion of nsp14. Manipulation of DDX1 expression, either by small interfering RNA-induced knockdown or by overexpression of a mutant DDX1 protein, confirmed that this interaction may enhance IBV replication. This study reveals that DDX1 contributes to efficient coronavirus replication in cell culture.</AbstractText>
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