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 Hui, E.
Right arrow Articles by Rochon, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hui, E.
Right arrow Articles by Rochon, D.

 Previous Article  |  Next Article 

Journal of Virology, June 2006, p. 5968-5975, Vol. 80, No. 12
0022-538X/06/$08.00+0     doi:10.1128/JVI.02485-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Evaluation of the Roles of Specific Regions of the Cucumber Necrosis Virus Coat Protein Arm in Particle Accumulation and Fungus Transmission

Elizabeth Hui1 and D'Ann Rochon1,2*

Faculty of Land and Food Systems, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada,1 Agriculture and Agri-Food Canada, Pacific Agri-Food Research Centre, Summerland, British Columbia V0H 1Z0, Canada2

Received 25 November 2005/ Accepted 9 March 2006

The Cucumber necrosis virus (CNV) particle is a T=3 icosahedron composed of 180 identical coat protein (CP) subunits. Each CP subunit includes a 34-amino-acid (aa) arm which connects the RNA binding and shell domains. The arm is comprised of an 18-aa "ß" region and a 16-aa "{varepsilon}" region, with the former contributing to a ß-annular structure involved in particle stability and the latter contributing to quasiequivalence and virion RNA binding. Previous work has shown that specific regions of the CNV capsid play important roles in transmission by zoospores of the fungal vector Olpidium bornovanus and that particle expansion is essential for this process. To assess the importance of the two arm regions in particle accumulation, stability, and virus transmission, five CP arm deletion mutants were constructed. Our findings indicate that ß(–) mutants are capable of producing particles in plants; however, the arm(–) and {varepsilon}(–) mutants are not. In addition, ß(–) particles bind zoospores less efficiently than wild-type CNV and are not fungally transmissible. ß(–) particles are also less thermally stable and disassemble under swelling conditions. Our finding that ß(–) mutants can accumulate in plants suggests that other features of the virion, such as RNA/CP interactions, may also be important for particle stability.

* Corresponding author. Mailing address: Agriculture and Agri-Food Canada, Pacific Agri-Food Research Centre, Summerland, BC V0H 1Z0, Canada. Phone: (250) 494-6394. Fax: (250) 494-0755. E-mail: rochonda{at}agr.gc.ca.

Journal of Virology, June 2006, p. 5968-5975, Vol. 80, No. 12
0022-538X/06/$08.00+0     doi:10.1128/JVI.02485-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Kakani, K., Reade, R., Katpally, U., Smith, T., Rochon, D. (2008). Induction of Particle Polymorphism by Cucumber Necrosis Virus Coat Protein Mutants In Vivo. J. Virol. 82: 1547-1557 [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»