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 Taliansky, M.
Right arrow Articles by Oparka, K. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Taliansky, M.
Right arrow Articles by Oparka, K. J.

 Previous Article  |  Next Article 

Journal of Virology, March 2003, p. 3031-3040, Vol. 77, No. 5
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.5.3031-3040.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

An Umbraviral Protein, Involved in Long-Distance RNA Movement, Binds Viral RNA and Forms Unique, Protective Ribonucleoprotein Complexes

Michael Taliansky,* Ian M. Roberts, Natalia Kalinina,{dagger} Eugene V. Ryabov,{ddagger} Shri Krishna Raj,§ David J. Robinson, and Karl J. Oparka

Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, United Kingdom

Received 20 September 2002/ Accepted 5 December 2002

Umbraviruses are different from most other viruses in that they do not encode a conventional capsid protein (CP); therefore, no recognizable virus particles are formed in infected plants. Their lack of a CP is compensated for by the ORF3 protein, which fulfils functions that are provided by the CPs of other viruses, such as protection and long-distance movement of viral RNA. When the Groundnut rosette virus (GRV) ORF3 protein was expressed from Tobacco mosaic virus (TMV) in place of the TMV CP [TMV(ORF3)], in infected cells it interacted with the TMV RNA to form filamentous ribonucleoprotein (RNP) particles that had elements of helical structure but were not as uniform as classical virions. These RNP particles were observed in amorphous inclusions in the cytoplasm, where they were embedded within an electron-dense matrix material. The inclusions were detected in all types of cells and were abundant in phloem-associated cells, in particular companion cells and immature sieve elements. RNP-containing complexes similar in appearance to the inclusions were isolated from plants infected with TMV(ORF3) or with GRV itself. In vitro, the ORF3 protein formed oligomers and bound RNA in a manner consistent with its role in the formation of RNP complexes. It is suggested that the cytoplasmic RNP complexes formed by the ORF3 protein serve to protect viral RNA and may be the form in which it moves through the phloem. Thus, the RNP particles detected here represent a novel structure which may be used by umbraviruses as an alternative to classical virions.

* Corresponding author. Mailing address: Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, United Kingdom. Phone: 44-(0)1382-562731. Fax: 44-(0)1382-562426. E-mail: mtalia{at}scri.sari.ac.uk.

{dagger} Permanent address: A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia.

{ddagger} Present address: Horticulture Research International-East Malling, West Malling, Kent ME19 6BJ, United Kingdom.

§ Permanent address: Plant Virus Laboratory, National Botanical Research Institute, Lucknow-226001, India.

Journal of Virology, March 2003, p. 3031-3040, Vol. 77, No. 5
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.5.3031-3040.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Rancurel, C., Khosravi, M., Dunker, A. K., Romero, P. R., Karlin, D. (2009). Overlapping Genes Produce Proteins with Unusual Sequence Properties and Offer Insight into De Novo Protein Creation. J. Virol. 83: 10719-10736 [Abstract] [Full Text]  
  • Kim, S. H., MacFarlane, S., Kalinina, N. O., Rakitina, D. V., Ryabov, E. V., Gillespie, T., Haupt, S., Brown, J. W. S., Taliansky, M. (2007). Interaction of a plant virus-encoded protein with the major nucleolar protein fibrillarin is required for systemic virus infection. Proc. Natl. Acad. Sci. USA 104: 11115-11120 [Abstract] [Full Text]  
  • Gopinath, K., Kao, C. C. (2007). Replication-Independent Long-Distance Trafficking by Viral RNAs in Nicotiana benthamiana. Plant Cell 19: 1179-1191 [Abstract] [Full Text]  
  • Leshchiner, A. D., Solovyev, A. G., Morozov, S. Yu., Kalinina, N. O. (2006). A minimal region in the NTPase/helicase domain of the TGBp1 plant virus movement protein is responsible for ATPase activity and cooperative RNA binding.. J. Gen. Virol. 87: 3087-3095 [Abstract] [Full Text]  
  • Valli, A., Martin-Hernandez, A. M., Lopez-Moya, J. J., Garcia, J. A. (2006). RNA Silencing Suppression by a Second Copy of the P1 Serine Protease of Cucumber Vein Yellowing Ipomovirus, a Member of the Family Potyviridae That Lacks the Cysteine Protease HCPro.. J. Virol. 80: 10055-10063 [Abstract] [Full Text]  
  • Ryabov, E. V., Kim, S. H., Taliansky, M. (2004). Identification of a nuclear localization signal and nuclear export signal of the umbraviral long-distance RNA movement protein. J. Gen. Virol. 85: 1329-1333 [Abstract] [Full Text]  
  • Taliansky, M. E., Robinson, D. J. (2003). Molecular biology of umbraviruses: phantom warriors. J. Gen. Virol. 84: 1951-1960 [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»