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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| Format: | Thesis |
| Language: | English English |
| Published: |
2003
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| Online Access: | http://psasir.upm.edu.my/id/eprint/9561/ http://psasir.upm.edu.my/id/eprint/9561/1/FSAS_2003_21_A.pdf |
| _version_ | 1848841180209479680 |
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| author | Kho, Chiew Ling |
| author_facet | Kho, Chiew Ling |
| author_sort | Kho, Chiew Ling |
| building | UPM Institutional Repository |
| collection | Online Access |
| 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. |
| first_indexed | 2025-11-15T07:39:08Z |
| format | Thesis |
| id | upm-9561 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English English |
| last_indexed | 2025-11-15T07:39:08Z |
| publishDate | 2003 |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-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. Newcastle disease virus. Viruses - Reproduction. English |
| 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 |
| title | 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_short | 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 |
| topic | Newcastle disease virus. Viruses - Reproduction. |
| url | http://psasir.upm.edu.my/id/eprint/9561/ http://psasir.upm.edu.my/id/eprint/9561/1/FSAS_2003_21_A.pdf |