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The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world.

Identifieur interne : 002F28 ( PubMed/Curation ); précédent : 002F27; suivant : 002F29

The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world.

Auteurs : Marie-Pierre Egloff [France] ; François Ferron ; Valérie Campanacci ; Sonia Longhi ; Corinne Rancurel ; Hélène Dutartre ; Eric J. Snijder ; Alexander E. Gorbalenya ; Christian Cambillau ; Bruno Canard

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2004.

RBID : pubmed:15007178

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Crystallography, X-Ray, DNA, Single-Stranded (metabolism), Molecular Sequence Data, Protein Structure, Tertiary, RNA (metabolism), RNA-Binding Proteins (genetics), RNA-Binding Proteins (metabolism), SARS Virus (genetics), SARS Virus (metabolism), Sequence Analysis, Protein, Severe Acute Respiratory Syndrome (metabolism), Severe Acute Respiratory Syndrome (virology), Viral Proteins (genetics), Viral Proteins (metabolism).
MESH :
- chemical , genetics : RNA-Binding Proteins, Viral Proteins.
- chemical , metabolism : DNA, Single-Stranded, RNA, RNA-Binding Proteins, Viral Proteins.
- genetics : SARS Virus.
- metabolism : SARS Virus, Severe Acute Respiratory Syndrome.
- virology : Severe Acute Respiratory Syndrome.
- Amino Acid Sequence, Crystallography, X-Ray, Molecular Sequence Data, Protein Structure, Tertiary, Sequence Analysis, Protein.

Abstract

The recently identified etiological agent of the severe acute respiratory syndrome (SARS) belongs to Coronaviridae (CoV), a family of viruses replicating by a poorly understood mechanism. Here, we report the crystal structure at 2.7-A resolution of nsp9, a hitherto uncharacterized subunit of the SARS-CoV replicative polyproteins. We show that SARS-CoV nsp9 is a single-stranded RNA-binding protein displaying a previously unreported, oligosaccharide/oligonucleotide fold-like fold. The presence of this type of protein has not been detected in the replicative complexes of RNA viruses, and its presence may reflect the unique and complex CoV viral replication/transcription machinery.

DOI: 10.1073/pnas.0307877101
PubMed: 15007178

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Le document en format XML

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<front><div type="abstract" xml:lang="en">The recently identified etiological agent of the severe acute respiratory syndrome (SARS) belongs to Coronaviridae (CoV), a family of viruses replicating by a poorly understood mechanism. Here, we report the crystal structure at 2.7-A resolution of nsp9, a hitherto uncharacterized subunit of the SARS-CoV replicative polyproteins. We show that SARS-CoV nsp9 is a single-stranded RNA-binding protein displaying a previously unreported, oligosaccharide/oligonucleotide fold-like fold. The presence of this type of protein has not been detected in the replicative complexes of RNA viruses, and its presence may reflect the unique and complex CoV viral replication/transcription machinery.</div>
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The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world.

The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world.

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