Peptide domain involved in the interaction between membrane protein and nucleocapsid protein of SARS-associated coronavirus.
Identifieur interne : 002612 ( PubMed/Corpus ); précédent : 002611; suivant : 002613Peptide domain involved in the interaction between membrane protein and nucleocapsid protein of SARS-associated coronavirus.
Auteurs : Xiaonan Fang ; Linbai Ye ; Khalid Amine Timani ; Shanshan Li ; Yingchun Zen ; Meng Zhao ; Hong Zheng ; Zhenghui WuSource :
- Journal of biochemistry and molecular biology [ 1225-8687 ] ; 2005.
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
Links to Exploration step
pubmed:16053703Le 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><nlm:affiliation>State Key Laboratory of Virology, College of Life Science, Wuhan University, Wuhan, Hubei 430072, China.</nlm:affiliation>
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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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<author><name sortKey="Fang, Xiaonan" sort="Fang, Xiaonan" uniqKey="Fang X" first="Xiaonan" last="Fang">Xiaonan Fang</name>
<affiliation><nlm:affiliation>State Key Laboratory of Virology, College of Life Science, Wuhan University, Wuhan, Hubei 430072, China.</nlm:affiliation>
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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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<term>Glutathione Transferase (genetics)</term>
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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>
<term>Protein Structure, Tertiary</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (isolation & purification)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>SARS Virus (metabolism)</term>
<term>Sequence Homology, Amino Acid</term>
<term>Viral Matrix Proteins (metabolism)</term>
<term>Virus Assembly</term>
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<term>Recombinant Proteins</term>
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<term>Viral Matrix Proteins</term>
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<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Membrane Fusion</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Protein Interaction Mapping</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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<Title>Journal of biochemistry and molecular biology</Title>
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<ArticleTitle>Peptide domain involved in the interaction between membrane protein and nucleocapsid protein of SARS-associated coronavirus.</ArticleTitle>
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<Abstract><AbstractText>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.</AbstractText>
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