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J Gen Virol 90 (2009), 392-397; DOI 10.1099/vir.0.005710-0

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Short Communication

Mutagenesis of the nucleocapsid protein of Nipah virus involved in capsid assembly

Swee Tin Ong1, Khatijah Yusoff1,2, Chiew Ling Kho3, Janna Ong Abdullah1 and Wen Siang Tan1,2

1 Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia
2 Institute of Bioscience, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia
3 Faculty of Engineering and Science, Universiti Tunku Abdul Rahman, UTAR Complex, Jalan Genting Kelang, 53300 Setapak, Kuala Lumpur, Malaysia

Correspondence
Wen Siang Tan
wstan{at}biotech.upm.edu.my

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.

A supplementary table showing the primers used in this study is available with the online version of this paper.






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