Cover Image

Oligomerization state of the multimerization domain of Nipah virus phosphoprotein

Oligomerization of the phospho (P) proteins of paramyxoviruses plays important roles in the viral genome replication and transcription. The multimerization domain of the P proteins (PMD) was found to be responsible and sufficient for the oligomerization process. However, the oligomeric status of Nip...

Full description

Saved in:
Bibliographic Details
Main Authors: Salvamani, Shamala, Goh, Zee Hong, Ho, Kok Lian, Tey, Beng Ti, Tan, Wen Siang
Format: Article
Language:English
Published: Elsevier 2013
Online Access:http://psasir.upm.edu.my/id/eprint/29460/1/Oligomerization%20state%20of%20the%20multimerization%20domain%20of%20Nipah%20virus%20phosphoprotein.pdf
http://psasir.upm.edu.my/id/eprint/29460/
http://www.sciencedirect.com/science/article/pii/S1359511313003954
Tags: Add Tag
No Tags, Be the first to tag this record!
id my.upm.eprints.29460
record_format eprints
spelling my.upm.eprints.294602016-07-12T09:35:19Z http://psasir.upm.edu.my/id/eprint/29460/ Oligomerization state of the multimerization domain of Nipah virus phosphoprotein Salvamani, Shamala Goh, Zee Hong Ho, Kok Lian Tey, Beng Ti Tan, Wen Siang Oligomerization of the phospho (P) proteins of paramyxoviruses plays important roles in the viral genome replication and transcription. The multimerization domain of the P proteins (PMD) was found to be responsible and sufficient for the oligomerization process. However, the oligomeric status of Nipah virus (NiV) P protein is still unknown. Therefore, the aim of this study was to produce the PMD region of NiV in bacteria in order to determine the oligomeric status of the P protein. The NiV PMD region was cloned into pTrcHis2-TOPO vector and expressed in Escherichia coli. SDS-PAGE and Western blot analysis confirmed the protein expression upon IPTG induction at 37 °C for 5 h. Immobilized metal affinity chromatography (IMAC) purification was developed to purify the recombinant histidine-tagged NiV PMD which yielded a purity of 97%. Chemical cross-linking revealed that the PMD of NiV formed tetramer. The stability of the oligomer was studied with dynamic light scattering while mass spectrometry confirmed the exact molecular masses of the cross-linked products. Circular dichroism analysis revealed that the NiV PMD contained high α-helical content (55%) suggesting the presence of a coiled coil structure. Elsevier 2013-10 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/29460/1/Oligomerization%20state%20of%20the%20multimerization%20domain%20of%20Nipah%20virus%20phosphoprotein.pdf Salvamani, Shamala and Goh, Zee Hong and Ho, Kok Lian and Tey, Beng Ti and Tan, Wen Siang (2013) Oligomerization state of the multimerization domain of Nipah virus phosphoprotein. Process Biochemistry, 48 (10). pp. 1476-1480. ISSN 1359-5113; ESSN: 1873-3298 http://www.sciencedirect.com/science/article/pii/S1359511313003954 10.1016/j.procbio.2013.07.012
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
description Oligomerization of the phospho (P) proteins of paramyxoviruses plays important roles in the viral genome replication and transcription. The multimerization domain of the P proteins (PMD) was found to be responsible and sufficient for the oligomerization process. However, the oligomeric status of Nipah virus (NiV) P protein is still unknown. Therefore, the aim of this study was to produce the PMD region of NiV in bacteria in order to determine the oligomeric status of the P protein. The NiV PMD region was cloned into pTrcHis2-TOPO vector and expressed in Escherichia coli. SDS-PAGE and Western blot analysis confirmed the protein expression upon IPTG induction at 37 °C for 5 h. Immobilized metal affinity chromatography (IMAC) purification was developed to purify the recombinant histidine-tagged NiV PMD which yielded a purity of 97%. Chemical cross-linking revealed that the PMD of NiV formed tetramer. The stability of the oligomer was studied with dynamic light scattering while mass spectrometry confirmed the exact molecular masses of the cross-linked products. Circular dichroism analysis revealed that the NiV PMD contained high α-helical content (55%) suggesting the presence of a coiled coil structure.
format Article
author Salvamani, Shamala
Goh, Zee Hong
Ho, Kok Lian
Tey, Beng Ti
Tan, Wen Siang
spellingShingle Salvamani, Shamala
Goh, Zee Hong
Ho, Kok Lian
Tey, Beng Ti
Tan, Wen Siang
Oligomerization state of the multimerization domain of Nipah virus phosphoprotein
author_facet Salvamani, Shamala
Goh, Zee Hong
Ho, Kok Lian
Tey, Beng Ti
Tan, Wen Siang
author_sort Salvamani, Shamala
title Oligomerization state of the multimerization domain of Nipah virus phosphoprotein
title_short Oligomerization state of the multimerization domain of Nipah virus phosphoprotein
title_full Oligomerization state of the multimerization domain of Nipah virus phosphoprotein
title_fullStr Oligomerization state of the multimerization domain of Nipah virus phosphoprotein
title_full_unstemmed Oligomerization state of the multimerization domain of Nipah virus phosphoprotein
title_sort oligomerization state of the multimerization domain of nipah virus phosphoprotein
publisher Elsevier
publishDate 2013
url http://psasir.upm.edu.my/id/eprint/29460/1/Oligomerization%20state%20of%20the%20multimerization%20domain%20of%20Nipah%20virus%20phosphoprotein.pdf
http://psasir.upm.edu.my/id/eprint/29460/
http://www.sciencedirect.com/science/article/pii/S1359511313003954
_version_ 1643829766952845312
score 13.211869

Similar Items