Mutagenesis of the nucleocapsid protein of nipah virus involved in capsid assembly.

• Main Authors: Swee, Tin Ong, Yusoff, Khatijah, Chiew, Ling Kho, Abdullah, Janna Ong, Wen, Siang Tan
• Format: Article
• Language: English
• Published: Society for General Microbiology 2009
• Online Access: http://psasir.upm.edu.my/id/eprint/15765/

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.