Nucleocapsid (NP) and Phospho-(P) Proteins of Newcastle Disease Virus: Identification of Regions on NP That Form Particles and Interact with P

The nucleocapsid protein ( NP) of Newcastle disease virus (NDV) plays an important role in the replication of the viral genomic RNA. The NP is closely associated with the viral phosphoprotein ( P) and this association is crucial in ensuring the specific binding ofNP to the viral RNA. In order to...

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Main Author:	Kho, Chiew Ling
Format:	Thesis
Language:	English English
Published:	2003
Subjects:	Newcastle disease virus. Viruses - Reproduction.
Online Access:	http://psasir.upm.edu.my/id/eprint/9561/1/FSAS_2003_21_A.pdf
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id	my-upm-ir.9561
record_format	uketd_dc
spelling	my-upm-ir.95612012-08-27T08:09:29Z Nucleocapsid (NP) and Phospho-(P) Proteins of Newcastle Disease Virus: Identification of Regions on NP That Form Particles and Interact with P 2003-05 Kho, Chiew Ling The nucleocapsid protein ( NP) of Newcastle disease virus (NDV) plays an important role in the replication of the viral genomic RNA. The NP is closely associated with the viral phosphoprotein ( P) and this association is crucial in ensuring the specific binding ofNP to the viral RNA. In order to have a better understanding of the structure and functions of the NP, deletion mutagenesis was carried out to characterise and localise regions involved in NP-NP and NP-P interactions. The NP and a fusion derivative (NPcfus) containing a hexa histidine tag at its C-terminus were produced abundantly in Escherichia coli. These proteins were fractionated on sucrose gradient centrifugation and microscopic analysis showed that both the NP and NP cfus proteins self-assembled predominantly into ring-like particles with the diameter of 24 ± 2 nm around a central hole of 7 ± 1 nm. Some of these ring-like particles stacked together to form herringbonelike particles which are heterogenous in length with a diameter of 20 ± 2 nm and a central hollow of 5 ± 1 nm. Fusion of the C-terminal end to 29 amino acids inclusive of the myc epitope and His-tag did not impair ring assembly but inhibit the formation of the long herringbone particles. Immunogold labelling of the ring-like particles with the anti-myc antibody showed that the Cterminus of the NPcfus protein is exposed on the surface of the particles. Newcastle disease virus. Viruses - Reproduction. 2003-05 Thesis http://psasir.upm.edu.my/id/eprint/9561/ http://psasir.upm.edu.my/id/eprint/9561/1/FSAS_2003_21_A.pdf application/pdf en public phd doctoral Universiti Putra Malaysia Newcastle disease virus. Viruses - Reproduction. Faculty of Science and Environmental Studies English
institution	Universiti Putra Malaysia
collection	PSAS Institutional Repository
language	English English
topic	Newcastle disease virus. Viruses - Reproduction.
spellingShingle	Newcastle disease virus. Viruses - Reproduction. Kho, Chiew Ling Nucleocapsid (NP) and Phospho-(P) Proteins of Newcastle Disease Virus: Identification of Regions on NP That Form Particles and Interact with P
description	The nucleocapsid protein ( NP) of Newcastle disease virus (NDV) plays an important role in the replication of the viral genomic RNA. The NP is closely associated with the viral phosphoprotein ( P) and this association is crucial in ensuring the specific binding ofNP to the viral RNA. In order to have a better understanding of the structure and functions of the NP, deletion mutagenesis was carried out to characterise and localise regions involved in NP-NP and NP-P interactions. The NP and a fusion derivative (NPcfus) containing a hexa histidine tag at its C-terminus were produced abundantly in Escherichia coli. These proteins were fractionated on sucrose gradient centrifugation and microscopic analysis showed that both the NP and NP cfus proteins self-assembled predominantly into ring-like particles with the diameter of 24 ± 2 nm around a central hole of 7 ± 1 nm. Some of these ring-like particles stacked together to form herringbonelike particles which are heterogenous in length with a diameter of 20 ± 2 nm and a central hollow of 5 ± 1 nm. Fusion of the C-terminal end to 29 amino acids inclusive of the myc epitope and His-tag did not impair ring assembly but inhibit the formation of the long herringbone particles. Immunogold labelling of the ring-like particles with the anti-myc antibody showed that the Cterminus of the NPcfus protein is exposed on the surface of the particles.
format	Thesis
qualification_name	Doctor of Philosophy (PhD.)
qualification_level	Doctorate
author	Kho, Chiew Ling
author_facet	Kho, Chiew Ling
author_sort	Kho, Chiew Ling
title	Nucleocapsid (NP) and Phospho-(P) Proteins of Newcastle Disease Virus: Identification of Regions on NP That Form Particles and Interact with P
title_short	Nucleocapsid (NP) and Phospho-(P) Proteins of Newcastle Disease Virus: Identification of Regions on NP That Form Particles and Interact with P
title_full	Nucleocapsid (NP) and Phospho-(P) Proteins of Newcastle Disease Virus: Identification of Regions on NP That Form Particles and Interact with P
title_fullStr	Nucleocapsid (NP) and Phospho-(P) Proteins of Newcastle Disease Virus: Identification of Regions on NP That Form Particles and Interact with P
title_full_unstemmed	Nucleocapsid (NP) and Phospho-(P) Proteins of Newcastle Disease Virus: Identification of Regions on NP That Form Particles and Interact with P
title_sort	nucleocapsid (np) and phospho-(p) proteins of newcastle disease virus: identification of regions on np that form particles and interact with p
granting_institution	Universiti Putra Malaysia
granting_department	Faculty of Science and Environmental Studies
publishDate	2003
url	http://psasir.upm.edu.my/id/eprint/9561/1/FSAS_2003_21_A.pdf
_version_	1747810981288869888

Nucleocapsid (NP) and Phospho-(P) Proteins of Newcastle Disease Virus: Identification of Regions on NP That Form Particles and Interact with P

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