SrasV1, PubMed, Curation, bibRecord, 002612

Peptide domain involved in the interaction between membrane protein and nucleocapsid protein of SARS-associated coronavirus.

Identifieur interne : 002612 ( PubMed/Curation ); précédent : 002611; suivant : 002613

Peptide domain involved in the interaction between membrane protein and nucleocapsid protein of SARS-associated coronavirus.

Auteurs : Xiaonan Fang [République populaire de Chine] ; Linbai Ye ; Khalid Amine Timani ; Shanshan Li ; Yingchun Zen ; Meng Zhao ; Hong Zheng ; Zhenghui Wu

Source :

Journal of biochemistry and molecular biology [ 1225-8687 ] ; 2005.

RBID : pubmed:16053703

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Glutathione Transferase (genetics), Glutathione Transferase (metabolism), Membrane Fusion (physiology), Molecular Sequence Data, Nucleocapsid Proteins (metabolism), Protein Binding, Protein Interaction Mapping, Protein Structure, Tertiary, Recombinant Proteins (genetics), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), SARS Virus (metabolism), Sequence Homology, Amino Acid, Viral Matrix Proteins (metabolism), Virus Assembly.
MESH :
- chemical , genetics : Glutathione Transferase, Recombinant Proteins.
- chemical , isolation & purification : Recombinant Proteins.
- chemical , metabolism : Glutathione Transferase, Nucleocapsid Proteins, Recombinant Proteins, Viral Matrix Proteins.
- metabolism : SARS Virus.
- physiology : Membrane Fusion.
- Amino Acid Sequence, Molecular Sequence Data, Protein Binding, Protein Interaction Mapping, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Virus Assembly.

Abstract

Severe acute respiratory syndrome (SARS) is an emerging infectious disease associated with a novel coronavirus (CoV) that was identified and molecularly characterized in 2003. Previous studies on various coronaviruses indicate that protein-protein interactions amongst various coronavirus proteins are critical for viral assembly and morphogenesis. It is necessary to elucidate the molecular mechanism of SARS-CoV replication and rationalize the anti-SARS therapeutic intervention. In this study, we employed an in vitro GST pull-down assay to investigate the interaction between the membrane (M) and the nucleocapsid (N) proteins. Our results show that the interaction between the M and N proteins does take place in vitro. Moreover, we provide an evidence that 12 amino acids domain (194-205) in the M protein is responsible for binding to N protein. Our work will help shed light on the molecular mechanism of the virus assembly and provide valuable information pertaining to rationalization of future anti-viral strategies.

DOI: 10.5483/bmbrep.2005.38.4.381
PubMed: 16053703

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Le document en format XML

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<author><name sortKey="Fang, Xiaonan" sort="Fang, Xiaonan" uniqKey="Fang X" first="Xiaonan" last="Fang">Xiaonan Fang</name>
<affiliation wicri:level="1"><nlm:affiliation>State Key Laboratory of Virology, College of Life Science, Wuhan University, Wuhan, Hubei 430072, China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>State Key Laboratory of Virology, College of Life Science, Wuhan University, Wuhan, Hubei 430072</wicri:regionArea>
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<author><name sortKey="Ye, Linbai" sort="Ye, Linbai" uniqKey="Ye L" first="Linbai" last="Ye">Linbai Ye</name>
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<author><name sortKey="Timani, Khalid Amine" sort="Timani, Khalid Amine" uniqKey="Timani K" first="Khalid Amine" last="Timani">Khalid Amine Timani</name>
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<author><name sortKey="Li, Shanshan" sort="Li, Shanshan" uniqKey="Li S" first="Shanshan" last="Li">Shanshan Li</name>
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<author><name sortKey="Zen, Yingchun" sort="Zen, Yingchun" uniqKey="Zen Y" first="Yingchun" last="Zen">Yingchun Zen</name>
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<author><name sortKey="Zhao, Meng" sort="Zhao, Meng" uniqKey="Zhao M" first="Meng" last="Zhao">Meng Zhao</name>
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<author><name sortKey="Zheng, Hong" sort="Zheng, Hong" uniqKey="Zheng H" first="Hong" last="Zheng">Hong Zheng</name>
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<author><name sortKey="Wu, Zhenghui" sort="Wu, Zhenghui" uniqKey="Wu Z" first="Zhenghui" last="Wu">Zhenghui Wu</name>
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<term>Membrane Fusion (physiology)</term>
<term>Molecular Sequence Data</term>
<term>Nucleocapsid Proteins (metabolism)</term>
<term>Protein Binding</term>
<term>Protein Interaction Mapping</term>
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<term>Glutathione transferase (génétique)</term>
<term>Glutathione transferase (métabolisme)</term>
<term>Liaison aux protéines</term>
<term>Protéines de la matrice virale (métabolisme)</term>
<term>Protéines nucléocapside (métabolisme)</term>
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<term>Virus du SRAS (métabolisme)</term>
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<term>Viral Matrix Proteins</term>
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<term>Protéines recombinantes</term>
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<term>Protéines de la matrice virale</term>
<term>Protéines nucléocapside</term>
<term>Protéines recombinantes</term>
<term>Virus du SRAS</term>
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<term>Molecular Sequence Data</term>
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<term>Protein Interaction Mapping</term>
<term>Protein Structure, Tertiary</term>
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<term>Liaison aux protéines</term>
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) is an emerging infectious disease associated with a novel coronavirus (CoV) that was identified and molecularly characterized in 2003. Previous studies on various coronaviruses indicate that protein-protein interactions amongst various coronavirus proteins are critical for viral assembly and morphogenesis. It is necessary to elucidate the molecular mechanism of SARS-CoV replication and rationalize the anti-SARS therapeutic intervention. In this study, we employed an in vitro GST pull-down assay to investigate the interaction between the membrane (M) and the nucleocapsid (N) proteins. Our results show that the interaction between the M and N proteins does take place in vitro. Moreover, we provide an evidence that 12 amino acids domain (194-205) in the M protein is responsible for binding to N protein. Our work will help shed light on the molecular mechanism of the virus assembly and provide valuable information pertaining to rationalization of future anti-viral strategies.</div>
</front>
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</Abstract>
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Peptide domain involved in the interaction between membrane protein and nucleocapsid protein of SARS-associated coronavirus.

Peptide domain involved in the interaction between membrane protein and nucleocapsid protein of SARS-associated coronavirus.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki