The "SARS-unique domain" (SUD) of SARS coronavirus is an oligo(G)-binding protein.
Identifieur interne : 003583 ( Main/Exploration ); précédent : 003582; suivant : 003584The "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. SchmidtSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2007.
Descripteurs français
- KwdFr :
- Nucléotides guanyliques (), Nucléotides guanyliques (métabolisme), Oligoribonucléotides (), Oligoribonucléotides (métabolisme), Protéines virales non structurales (), Protéines virales non structurales (métabolisme), RNA replicase (), RNA replicase (métabolisme), Structure tertiaire des protéines, Virus du SRAS (métabolisme).
- MESH :
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
Affiliations:
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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. 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Schmidt</name><name sortKey="Tech, Stefanie" sort="Tech, Stefanie" uniqKey="Tech S" first="Stefanie" last="Tech">Stefanie Tech</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Tan, Jinzhi" sort="Tan, Jinzhi" uniqKey="Tan J" first="Jinzhi" last="Tan">Jinzhi Tan</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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