SrasV1, Ncbi, Merge, bibRecord, 001B00

The "SARS-unique domain" (SUD) of SARS coronavirus is an oligo(G)-binding protein.

Identifieur interne : 001B00 ( Ncbi/Merge ); précédent : 001A99; suivant : 001B01

The "SARS-unique domain" (SUD) of SARS coronavirus is an oligo(G)-binding protein.

Auteurs : Jinzhi Tan [Allemagne] ; Yuri Kusov ; Doris Mutschall ; Stefanie Tech ; Krishna Nagarajan ; Rolf Hilgenfeld ; Christian L. Schmidt

Source :

Biochemical and biophysical research communications [ 1090-2104 ] ; 2007.

RBID : pubmed:17976532

Descripteurs français

English descriptors

KwdEn :
- Guanine Nucleotides (chemistry), Guanine Nucleotides (metabolism), Oligoribonucleotides (chemistry), Oligoribonucleotides (metabolism), Protein Structure, Tertiary, RNA Replicase (chemistry), RNA Replicase (metabolism), SARS Virus (metabolism), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (metabolism).
MESH :
- chemical , chemistry : Guanine Nucleotides, Oligoribonucleotides, RNA Replicase, Viral Nonstructural Proteins.
- chemical , metabolism : Guanine Nucleotides, Oligoribonucleotides, RNA Replicase, Viral Nonstructural Proteins.
- metabolism : SARS Virus.
- Protein Structure, Tertiary.

Abstract

Caused by a new coronavirus, severe acute respiratory syndrome (SARS) is a highly contagious disease associated with significant fatality that emerged in 2003. The molecular cause of the unusually high human pathogenicity of the SARS coronavirus (SARS-CoV) is still unknown. In an effort to characterize molecular components of the virus that are absent in other coronaviruses, all of which are considerably less pathogenic for humans, we recombinantly produced the SARS-unique domain (SUD) within non-structural protein 3 (Nsp3) of SARS-CoV and characterized its nucleic-acid binding properties. Zone-interference gel electrophoresis and electrophoretic mobility shift assays revealed a specific affinity of SUD for oligo(G)-strings. A few such segments are present in the SARS-CoV genome, but also in mRNAs of host proteins involved in the regulation of signaling pathways. A putative role of SUD in virus-induced apoptosis or survival of host cells is discussed.

DOI: 10.1016/j.bbrc.2007.10.081
PubMed: 17976532

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Caused by a new coronavirus, severe acute respiratory syndrome (SARS) is a highly contagious disease associated with significant fatality that emerged in 2003. The molecular cause of the unusually high human pathogenicity of the SARS coronavirus (SARS-CoV) is still unknown. In an effort to characterize molecular components of the virus that are absent in other coronaviruses, all of which are considerably less pathogenic for humans, we recombinantly produced the SARS-unique domain (SUD) within non-structural protein 3 (Nsp3) of SARS-CoV and characterized its nucleic-acid binding properties. Zone-interference gel electrophoresis and electrophoretic mobility shift assays revealed a specific affinity of SUD for oligo(G)-strings. A few such segments are present in the SARS-CoV genome, but also in mRNAs of host proteins involved in the regulation of signaling pathways. A putative role of SUD in virus-induced apoptosis or survival of host cells is discussed.</div>
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{{Explor lien
   |wiki=    Sante
   |area=    SrasV1
   |flux=    Ncbi
   |étape=   Merge
   |type=    RBID
   |clé=     pubmed:17976532
   |texte=   The "SARS-unique domain" (SUD) of SARS coronavirus is an oligo(G)-binding protein.
}}

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The "SARS-unique domain" (SUD) of SARS coronavirus is an oligo(G)-binding protein.

The "SARS-unique domain" (SUD) of SARS coronavirus is an oligo(G)-binding protein.

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