Mutagenesis of the nucleocapsid protein of nipah virus involved in capsid assembly.
The nucleocapsid protein of Nipah virus produced in Escherichia coli assembled into herringbone-like particles. The amino- and carboxy-termini of the N protein were shortened progressively to define the minimum contiguous sequence involved in capsid assembly. The first 29 aa residues of the N protei...
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| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Society for General Microbiology
2009
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| Online Access: | http://psasir.upm.edu.my/id/eprint/15765/ |
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| Institution: | Universiti Putra Malaysia |
| Language: | English |
| Summary: | The nucleocapsid protein of Nipah virus produced in Escherichia coli assembled into herringbone-like particles. The amino- and carboxy-termini of the N protein were shortened progressively to define the minimum contiguous sequence involved in capsid assembly. The first 29 aa residues of the N protein are dispensable for capsid formation. The 128 carboxy-terminal residues do not play a role in the assembly of the herringbone-like particles. A region with amino acid residues 30–32 plays a crucial role in the formation of the capsid particle. Deletion of any of
the four conserved hydrophobic regions in the N protein impaired capsid formation. Replacement of the central conserved regions with the respective sequences from the Newcastle disease virus restored capsid formation. |
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