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: Swee, Tin Ong, Yusoff, Khatijah, Chiew, Ling Kho, Abdullah, Janna Ong, Wen, Siang Tan
Format: Article
Language:English
Published: Society for General Microbiology 2009
Subjects:
Online Access:http://psasir.upm.edu.my/id/eprint/15765/
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author Swee, Tin Ong
Yusoff, Khatijah
Chiew, Ling Kho
Abdullah, Janna Ong
Wen, Siang Tan
author_facet Swee, Tin Ong
Yusoff, Khatijah
Chiew, Ling Kho
Abdullah, Janna Ong
Wen, Siang Tan
author_sort Swee, Tin Ong
building UPM Institutional Repository
collection Online Access
description 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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spelling upm-157652014-09-17T08:10:36Z http://psasir.upm.edu.my/id/eprint/15765/ Mutagenesis of the nucleocapsid protein of nipah virus involved in capsid assembly. Swee, Tin Ong Yusoff, Khatijah Chiew, Ling Kho Abdullah, Janna Ong Wen, Siang Tan 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. Society for General Microbiology 2009 Article PeerReviewed Swee, Tin Ong and Yusoff, Khatijah and Chiew, Ling Kho and 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 Nipah virus - Research Mutagenesis Viruses 10.1099/vir.0.005710-0 English
spellingShingle Nipah virus - Research
Mutagenesis
Viruses
Swee, Tin Ong
Yusoff, Khatijah
Chiew, Ling Kho
Abdullah, Janna Ong
Wen, Siang Tan
Mutagenesis of the nucleocapsid protein of nipah virus involved in capsid assembly.
title Mutagenesis of the nucleocapsid protein of nipah virus involved in capsid assembly.
title_full Mutagenesis of the nucleocapsid protein of nipah virus involved in capsid assembly.
title_fullStr Mutagenesis of the nucleocapsid protein of nipah virus involved in capsid assembly.
title_full_unstemmed Mutagenesis of the nucleocapsid protein of nipah virus involved in capsid assembly.
title_short Mutagenesis of the nucleocapsid protein of nipah virus involved in capsid assembly.
title_sort mutagenesis of the nucleocapsid protein of nipah virus involved in capsid assembly.
topic Nipah virus - Research
Mutagenesis
Viruses
url http://psasir.upm.edu.my/id/eprint/15765/
http://psasir.upm.edu.my/id/eprint/15765/