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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
Online Access:http://psasir.upm.edu.my/id/eprint/9561/1/FSAS_2003_21_A.pdf
http://psasir.upm.edu.my/id/eprint/9561/
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spelling my.upm.eprints.95612012-08-27T08:09:29Z http://psasir.upm.edu.my/id/eprint/9561/ Nucleocapsid (NP) and Phospho-(P) Proteins of Newcastle Disease Virus: Identification of Regions on NP That Form Particles and Interact with P 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. 2003-05 Thesis NonPeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/9561/1/FSAS_2003_21_A.pdf Kho, Chiew Ling (2003) Nucleocapsid (NP) and Phospho-(P) Proteins of Newcastle Disease Virus: Identification of Regions on NP That Form Particles and Interact with P. PhD thesis, Universiti Putra Malaysia. English
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
English
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
author Kho, Chiew Ling
spellingShingle 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
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
publishDate 2003
url http://psasir.upm.edu.my/id/eprint/9561/1/FSAS_2003_21_A.pdf
http://psasir.upm.edu.my/id/eprint/9561/
_version_ 1643824351386009600
score 13.211869

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