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VHL negatively regulates SARS coronavirus replication by modulating nsp16 ubiquitination and stability.

Identifieur interne : 000D21 ( PubMed/Checkpoint ); précédent : 000D20; suivant : 000D22

VHL negatively regulates SARS coronavirus replication by modulating nsp16 ubiquitination and stability.

Auteurs : Xiao Yu [République populaire de Chine] ; Shuliang Chen [République populaire de Chine] ; Panpan Hou [République populaire de Chine] ; Min Wang [République populaire de Chine] ; Yu Chen [République populaire de Chine] ; Deyin Guo [République populaire de Chine]

Source :

Biochemical and biophysical research communications [ 1090-2104 ] ; 2015.

RBID : pubmed:25732088

Descripteurs français

English descriptors

KwdEn :
- Animals, Chlorocebus aethiops, Exoribonucleases (genetics), Exoribonucleases (metabolism), Host-Pathogen Interactions (physiology), Humans, Methyltransferases (chemistry), Methyltransferases (genetics), Methyltransferases (metabolism), Protein Stability, Proteolysis, Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), SARS Virus (genetics), SARS Virus (physiology), Two-Hybrid System Techniques, Ubiquitination, Vero Cells, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism), Virus Replication (physiology), Von Hippel-Lindau Tumor Suppressor Protein (genetics), Von Hippel-Lindau Tumor Suppressor Protein (metabolism).
MESH :
- chemical , chemistry : Methyltransferases, Recombinant Fusion Proteins, Viral Nonstructural Proteins.
- chemical , genetics : Exoribonucleases, Methyltransferases, Recombinant Fusion Proteins, Viral Nonstructural Proteins, Von Hippel-Lindau Tumor Suppressor Protein.
- chemical , metabolism : Exoribonucleases, Methyltransferases, Recombinant Fusion Proteins, Viral Nonstructural Proteins, Von Hippel-Lindau Tumor Suppressor Protein.
- genetics : SARS Virus.
- physiology : Host-Pathogen Interactions, SARS Virus, Virus Replication.
- Animals, Chlorocebus aethiops, Humans, Protein Stability, Proteolysis, Two-Hybrid System Techniques, Ubiquitination, Vero Cells.

Abstract

Eukaryotic cellular and most viral RNAs carry a 5'-terminal cap structure, a 5'-5' triphosphate linkage between the 5' end of the RNA and a guanosine nucleotide (cap-0). SARS coronavirus (SARS-CoV) nonstructural protein nsp16 functions as a methyltransferase, to methylate mRNA cap-0 structure at the ribose 2'-O position of the first nucleotide to form cap-1 structures. However, whether there is interplay between nsp16 and host proteins was not yet clear. In this report, we identified several potential cellular nsp16-interacting proteins from a human thymus cDNA library by yeast two-hybrid screening. VHL, one of these proteins, was proven to interact with nsp16 both in vitro and in vivo. Further studies showed that VHL can inhibit SARS-CoV replication by regulating nsp16 ubiquitination and promoting its degradation. Our results have revealed the role of cellular VHL in the regulation of SARS-CoV replication.

DOI: 10.1016/j.bbrc.2015.02.097
PubMed: 25732088

Affiliations:

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Eukaryotic cellular and most viral RNAs carry a 5'-terminal cap structure, a 5'-5' triphosphate linkage between the 5' end of the RNA and a guanosine nucleotide (cap-0). SARS coronavirus (SARS-CoV) nonstructural protein nsp16 functions as a methyltransferase, to methylate mRNA cap-0 structure at the ribose 2'-O position of the first nucleotide to form cap-1 structures. However, whether there is interplay between nsp16 and host proteins was not yet clear. In this report, we identified several potential cellular nsp16-interacting proteins from a human thymus cDNA library by yeast two-hybrid screening. VHL, one of these proteins, was proven to interact with nsp16 both in vitro and in vivo. Further studies showed that VHL can inhibit SARS-CoV replication by regulating nsp16 ubiquitination and promoting its degradation. Our results have revealed the role of cellular VHL in the regulation of SARS-CoV replication.</div>
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<Abstract><AbstractText>Eukaryotic cellular and most viral RNAs carry a 5'-terminal cap structure, a 5'-5' triphosphate linkage between the 5' end of the RNA and a guanosine nucleotide (cap-0). SARS coronavirus (SARS-CoV) nonstructural protein nsp16 functions as a methyltransferase, to methylate mRNA cap-0 structure at the ribose 2'-O position of the first nucleotide to form cap-1 structures. However, whether there is interplay between nsp16 and host proteins was not yet clear. In this report, we identified several potential cellular nsp16-interacting proteins from a human thymus cDNA library by yeast two-hybrid screening. VHL, one of these proteins, was proven to interact with nsp16 both in vitro and in vivo. Further studies showed that VHL can inhibit SARS-CoV replication by regulating nsp16 ubiquitination and promoting its degradation. Our results have revealed the role of cellular VHL in the regulation of SARS-CoV replication.</AbstractText>
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VHL negatively regulates SARS coronavirus replication by modulating nsp16 ubiquitination and stability.

VHL negatively regulates SARS coronavirus replication by modulating nsp16 ubiquitination and stability.

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