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Journal of Virology, February 2008, p. 1547-1557, Vol. 82, No. 3
0022-538X/08/$08.00+0     doi:10.1128/JVI.01976-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Induction of Particle Polymorphism by Cucumber Necrosis Virus Coat Protein Mutants In Vivo

Kishore Kakani,^1,# Ron Reade,^1,# Umesh Katpally,² Thomas Smith,² and D'Ann Rochon^1*

Agriculture and Agri-Food Canada, Pacific Agri-Food Research Centre, 4200 Hwy. 97, Box 5000, Summerland, British Columbia, Canada V0H 1Z0,¹ Donald Danforth Plant Science Center, 975 North Warson Road, St. Louis, Missouri 63132²

Received 7 September 2007/ Accepted 9 November 2007

The Cucumber necrosis virus (CNV) particle is a T=3 icosahedron consisting of 180 identical coat protein (CP) subunits. Plants infected with wild-type CNV accumulate a high number of T=3 particles, but other particle forms have not been observed. Particle polymorphism in several T=3 icosahedral viruses has been observed in vitro following the removal of an extended N-terminal region of the CP subunit. In the case of CNV, we have recently described the structure of T=1 particles that accumulate in planta during infection by a CNV mutant (R1+2) in which a large portion of the N-terminal RNA binding domain (R-domain) has been deleted. In this report we further describe properties of this mutant and other CP mutants that produce polymorphic particles. The T=1 particles produced by R1+2 mutants were found to encapsidate a 1.9-kb RNA species as well as smaller RNA species that are similar to previously described CNV defective interfering RNAs. Other R-domain mutants were found to encapsidate a range of specifically sized less-than-full-length CNV RNAs. Mutation of a conserved proline residue in the arm domain near its junction with the shell domain also influenced T=1 particle formation. The proportion of polymorphic particles increased when the mutation was incorporated into R-domain deletion mutants. Our results suggest that both the R-domain and the arm play important roles in the formation of T=3 particles. In addition, the encapsidation of specific CNV RNA species by individual mutants indicates that the R-domain plays a role in the nature of CNV RNA encapsidated in particles.

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* Corresponding author. Mailing address: Agriculture and Agri-Food Canada, Pacific Agri-Food Research Centre, 4200 Hwy. 97, Box 5000, Summerland, British Columbia, Canada V0H 1Z0. Phone: (250) 494-6394. Fax: (250) 494-0755. E-mail: rochonda{at}agr.gc.ca

Published ahead of print on 21 November 2007.

^# K. Kakani and R. Reade contributed equally to this work.

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Journal of Virology, February 2008, p. 1547-1557, Vol. 82, No. 3
0022-538X/08/$08.00+0     doi:10.1128/JVI.01976-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

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