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

Identifieur interne : 004726 ( Main/Exploration ); précédent : 004725; suivant : 004727

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 :

RBID : pubmed:16053703

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English descriptors

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


Affiliations:


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Le document en format XML

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<term>Membrane Fusion (physiology)</term>
<term>Molecular Sequence Data</term>
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<term>Recombinant Proteins (metabolism)</term>
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<term>Glutathione transferase (génétique)</term>
<term>Glutathione transferase (métabolisme)</term>
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<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>
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