Mutagenesis of the nucleocapsid protein of nipah virus involved in capsid assembly.
Swee, Tin Ong, Yusoff, Khatijah, Chiew, Ling Kho, Abdullah, Janna Ong and Wen, Siang Tan (2009) Mutagenesis of the nucleocapsid protein of nipah virus involved in capsid assembly. Journal of General Virology, 90 (2). pp. 392-397. ISSN 0022-1317
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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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