Please use this identifier to cite or link to this item:
https://doi.org/10.1016/j.virol.2007.04.029
DC Field | Value | |
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dc.title | The nonstructural protein 8 (nsp8) of the SARS coronavirus interacts with its ORF6 accessory protein | |
dc.contributor.author | Kumar, P. | |
dc.contributor.author | Gunalan, V. | |
dc.contributor.author | Liu, B. | |
dc.contributor.author | Chow, V.T.K. | |
dc.contributor.author | Druce, J. | |
dc.contributor.author | Birch, C. | |
dc.contributor.author | Catton, M. | |
dc.contributor.author | Fielding, B.C. | |
dc.contributor.author | Tan, Y.-J. | |
dc.contributor.author | Lal, S.K. | |
dc.date.accessioned | 2014-11-10T08:08:43Z | |
dc.date.available | 2014-11-10T08:08:43Z | |
dc.date.issued | 2007-09-30 | |
dc.identifier.citation | Kumar, P., Gunalan, V., Liu, B., Chow, V.T.K., Druce, J., Birch, C., Catton, M., Fielding, B.C., Tan, Y.-J., Lal, S.K. (2007-09-30). The nonstructural protein 8 (nsp8) of the SARS coronavirus interacts with its ORF6 accessory protein. Virology 366 (2) : 293-303. ScholarBank@NUS Repository. https://doi.org/10.1016/j.virol.2007.04.029 | |
dc.identifier.issn | 00426822 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/107627 | |
dc.description.abstract | Severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) caused a severe outbreak in several regions of the world in 2003. The SARS-CoV genome is predicted to contain 14 functional open reading frames (ORFs). The first ORF (1a and 1b) encodes a large polyprotein that is cleaved into nonstructural proteins (nsp). The other ORFs encode for four structural proteins (spike, membrane, nucleocapsid and envelope) as well as eight SARS-CoV-specific accessory proteins (3a, 3b, 6, 7a, 7b, 8a, 8b and 9b). In this report we have cloned the predicted nsp8 gene and the ORF6 gene of the SARS-CoV and studied their abilities to interact with each other. We expressed the two proteins as fusion proteins in the yeast two-hybrid system to demonstrate protein-protein interactions and tested the same using a yeast genetic cross. Further the strength of the interaction was measured by challenging growth of the positive interaction clones on increasing gradients of 2-amino trizole. The interaction was then verified by expressing both proteins separately in-vitro in a coupled-transcription translation system and by coimmunoprecipitation in mammalian cells. Finally, colocalization experiments were performed in SARS-CoV infected Vero E6 mammalian cells to confirm the nsp8-ORF6 interaction. To the best of our knowledge, this is the first report of the interaction between a SARS-CoV accessory protein and nsp8 and our findings suggest that ORF6 protein may play a role in virus replication. © 2007 Elsevier Inc. All rights reserved. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.virol.2007.04.029 | |
dc.source | Scopus | |
dc.subject | Accessory protein | |
dc.subject | Immunoprecipitation | |
dc.subject | Non structural protein | |
dc.subject | Protein-protein interaction | |
dc.subject | SARS coronavirus | |
dc.subject | Yeast two-hybrid system | |
dc.type | Article | |
dc.contributor.department | MICROBIOLOGY | |
dc.description.doi | 10.1016/j.virol.2007.04.029 | |
dc.description.sourcetitle | Virology | |
dc.description.volume | 366 | |
dc.description.issue | 2 | |
dc.description.page | 293-303 | |
dc.description.coden | VIRLA | |
dc.identifier.isiut | 000249769400006 | |
Appears in Collections: | Staff Publications |
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