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Characterization of the NSP6 protein product of rotavirus gene 11
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Rainsford, Edward W. and McCrae, Malcolm A. (2007) Characterization of the NSP6 protein product of rotavirus gene 11. Virus Research, Vol.130 (No.1-2). pp. 193-201. doi:10.1016/j.virusres.2007.06.011 ISSN 0168-1702.
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Official URL: http://dx.doi.org/10.1016/j.virusres.2007.06.011
Abstract
The 12kDa non-structural protein 6 (NSP6) is the least studied of the rotavirus proteins. In an attempt to further characterize this protein mono-specific antisera was generated using purified protein expressed in E. coli. Pulse/chase radio-labeling of virus infected cells was used to show that it is expressed at a steady but low rate throughout the virus replication cycle. In contrast to the other rotavirus non-structural proteins, NSP6 was found to have a high rate of turnover, being completely degraded within 2h of synthesis. NSP6 tagged with GFP was used to probe the intracellular distribution of the protein, perinuclear aggregates were observed in the cytoplasm of transfected cells. Following virus infection of these transfected cells the aggregates were seen to redistribute to the viroplasms. Consistent with its localization to the site of viral genome replication and packaging, NSP6 was found to be a sequence independent nucleic acid binding protein, with similar affinities for ssRNA and dsRNA.
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Subjects: | Q Science > QR Microbiology > QR355 Virology | ||||
| Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) > Biological Sciences ( -2010) | ||||
| Journal or Publication Title: | Virus Research | ||||
| Publisher: | Elsevier Science BV | ||||
| ISSN: | 0168-1702 | ||||
| Official Date: | December 2007 | ||||
| Dates: |
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| Volume: | Vol.130 | ||||
| Number: | No.1-2 | ||||
| Number of Pages: | 9 | ||||
| Page Range: | pp. 193-201 | ||||
| DOI: | 10.1016/j.virusres.2007.06.011 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access |
Data sourced from Thomson Reuters' Web of Knowledge
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