The multimerization/self-interaction of viral proteins is an important step in the process of viral assembly and maturation. Our previous study indicated that the severe acute respiratory syndrome-associated coronavirus (SARS-CoV) nucleocapsid protein forms self-multimers through a serine-arginine (SR)-rich motif (SSRSSSRSRGNSR) by using a mammalian two-hybrid system. To determine the biological relevance of this motif, we constructed a SARS-CoV reverse genetic construct by using a bacterial artificial chromosome (BAC)-based vector controlled by a T7 promoter; and subsequently deleted the SR-rich motif from the N gene. The mutated infectious clone showed reduced level of genome transcription and significantly reduced levels of the infectious virions. These results strongly suggest that the SR-rich motif is critical for effective virus replication.
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| rdfs:comment |
The multimerization/self-interaction of viral proteins is an important step in the process of viral assembly and maturation. Our previous study indicated that the severe acute respiratory syndrome-associated coronavirus (SARS-CoV) nucleocapsid protein forms self-multimers through a serine-arginine (SR)-rich motif (SSRSSSRSRGNSR) by using a mammalian two-hybrid system. To determine the biological relevance of this motif, we constructed a SARS-CoV reverse genetic construct by using a bacterial artificial chromosome (BAC)-based vector controlled by a T7 promoter; and subsequently deleted the SR-rich motif from the N gene. The mutated infectious clone showed reduced level of genome transcription and significantly reduced levels of the infectious virions. These results strongly suggest that the SR-rich motif is critical for effective virus replication.
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| skos:exactMatch | |
| uniprot:name |
Can. J. Microbiol.
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| uniprot:author |
Andonov A.,
Cao J.,
Cutts T.,
Grudesky E.,
He R.,
Li X.,
Tylor S.,
Van Domselaar G.
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| uniprot:date |
2009
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| uniprot:pages |
254-260
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| uniprot:title |
The SR-rich motif in SARS-CoV nucleocapsid protein is important for virus replication.
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| uniprot:volume |
55
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| dc-term:identifier |
doi:10.1139/W08-139
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