This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Miller, C. L.
Right arrow Articles by Nibert, M. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Miller, C. L.
Right arrow Articles by Nibert, M. L.

 Previous Article  |  Next Article 

Journal of Virology, April 2003, p. 4566-4576, Vol. 77, No. 8
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.8.4566-4576.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Reovirus {sigma}NS Protein Localizes to Inclusions through an Association Requiring the µNS Amino Terminus

Cathy L. Miller,1 Teresa J. Broering,1 John S. L. Parker,1 Michelle M. Arnold,1,2 and Max L. Nibert1,2*

Department of Microbiology and Molecular Genetics,1 Virology Training Program, Harvard Medical School, Boston, Massachusetts 021152

Received 11 October 2002/ Accepted 23 January 2003

Cells infected with mammalian reoviruses contain phase-dense inclusions, called viral factories, in which viral replication and assembly are thought to occur. The major reovirus nonstructural protein µNS forms morphologically similar phase-dense inclusions when expressed in the absence of other viral proteins, suggesting it is a primary determinant of factory formation. In this study we examined the localization of the other major reovirus nonstructural protein, {sigma}NS. Although {sigma}NS colocalized with µNS in viral factories during infection, it was distributed diffusely throughout the cell when expressed in the absence of µNS. When coexpressed with µNS, {sigma}NS was redistributed and colocalized with µNS inclusions, indicating that the two proteins associate in the absence of other viral proteins and suggesting that this association may mediate the localization of {sigma}NS to viral factories in infected cells. We have previously shown that µNS residues 1 to 40 or 41 are both necessary and sufficient for µNS association with the viral microtubule-associated protein µ2. In the present study we found that this same region of µNS is required for its association with {sigma}NS. We further dissected this region, identifying residues 1 to 13 of µNS as necessary for association with {sigma}NS, but not with µ2. Deletion of {sigma}NS residues 1 to 11, which we have previously shown to be required for RNA binding by that protein, resulted in diminished association of {sigma}NS with µNS. Furthermore, when treated with RNase, a large portion of {sigma}NS was released from µNS coimmunoprecipitates, suggesting that RNA contributes to their association. The results of this study provide further evidence that µNS plays a key role in forming the reovirus factories and recruiting other components to them.

* Corresponding author. Mailing address: Dept. of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Ave., Boston, MA 02115. Phone: (617) 645-3680. Fax: (617) 738-7664. E-mail: mnibert{at}hms.harvard.edu.

Journal of Virology, April 2003, p. 4566-4576, Vol. 77, No. 8
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.8.4566-4576.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Qin, Q., Hastings, C., Miller, C. L. (2009). Mammalian Orthoreovirus Particles Induce and Are Recruited into Stress Granules at Early Times Postinfection. J. Virol. 83: 11090-11101 [Abstract] [Full Text]  
  • Kobayashi, T., Ooms, L. S., Chappell, J. D., Dermody, T. S. (2009). Identification of Functional Domains in Reovirus Replication Proteins {micro}NS and {micro}2. J. Virol. 83: 2892-2906 [Abstract] [Full Text]  
  • Miller, C. L., Arnold, M. M., Broering, T. J., Eichwald, C., Kim, J., Dinoso, J. B., Nibert, M. L. (2007). Virus-derived Platforms for Visualizing Protein Associations inside Cells. Mol. Cell. Proteomics 6: 1027-1038 [Abstract] [Full Text]  
  • Murray, K. E., Nibert, M. L. (2007). Guanidine Hydrochloride Inhibits Mammalian Orthoreovirus Growth by Reversibly Blocking the Synthesis of Double-Stranded RNA. J. Virol. 81: 4572-4584 [Abstract] [Full Text]  
  • Kobayashi, T., Chappell, J. D., Danthi, P., Dermody, T. S. (2006). Gene-specific inhibition of reovirus replication by RNA interference.. J. Virol. 80: 9053-9063 [Abstract] [Full Text]  
  • Wei, T., Shimizu, T., Hagiwara, K., Kikuchi, A., Moriyasu, Y., Suzuki, N., Chen, H., Omura, T. (2006). Pns12 protein of Rice dwarf virus is essential for formation of viroplasms and nucleation of viral-assembly complexes. J. Gen. Virol. 87: 429-438 [Abstract] [Full Text]  
  • Broering, T. J., Arnold, M. M., Miller, C. L., Hurt, J. A., Joyce, P. L., Nibert, M. L. (2005). Carboxyl-Proximal Regions of Reovirus Nonstructural Protein {micro}NS Necessary and Sufficient for Forming Factory-Like Inclusions. J. Virol. 79: 6194-6206 [Abstract] [Full Text]  
  • Touris-Otero, F., Martinez-Costas, J., Vakharia, V. N., Benavente, J. (2005). Characterization of the nucleic acid-binding activity of the avian reovirus non-structural protein {sigma}NS. J. Gen. Virol. 86: 1159-1169 [Abstract] [Full Text]  
  • Miller, C. L., Parker, J. S. L., Dinoso, J. B., Piggott, C. D. S., Perron, M. J., Nibert, M. L. (2004). Increased Ubiquitination and Other Covariant Phenotypes Attributed to a Strain- and Temperature-Dependent Defect of Reovirus Core Protein {micro}2. J. Virol. 78: 10291-10302 [Abstract] [Full Text]  
  • Broering, T. J., Kim, J., Miller, C. L., Piggott, C. D. S., Dinoso, J. B., Nibert, M. L., Parker, J. S. L. (2004). Reovirus Nonstructural Protein {micro}NS Recruits Viral Core Surface Proteins and Entering Core Particles to Factory-Like Inclusions. J. Virol. 78: 1882-1892 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»