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Journal of Virology, October 2004, p. 11142-11151, Vol. 78, No. 20
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.20.11142-11151.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Avian Reovirus Temperature-Sensitive Mutant tsA12 Has a Lesion in Major Core Protein {sigma}A and Is Defective in Assembly

Wanhong Xu, Megan K. Patrick, Paul R. Hazelton, and Kevin M. Coombs*

Department of Medical Microbiology and Infectious Diseases, University of Manitoba, Winnipeg, Manitoba, Canada

Received 27 February 2004/ Accepted 18 May 2004

Members of our laboratory previously generated and described a set of avian reovirus (ARV) temperature-sensitive (ts) mutants and assigned 11 of them to 7 of the 10 expected recombination groups, named A through G (M. Patrick, R. Duncan, and K. M. Coombs, Virology 284:113-122, 2001). This report presents a more detailed analysis of two of these mutants (tsA12 and tsA146), which were previously assigned to recombination group A. The capacities of tsA12 and tsA146 to replicate at a variety of temperatures were determined. Morphological analyses indicated that cells infected with tsA12 at a nonpermissive temperature produced ~100-fold fewer particles than cells infected at a permissive temperature and accumulated core particles. Cells infected with tsA146 at a nonpermissive temperature also produced ~100-fold fewer particles, a larger proportion of which were intact virions. We crossed tsA12 with ARV strain 176 to generate reassortant clones and used them to map the temperature-sensitive lesion in tsA12 to the S2 gene. S2 encodes the major core protein {sigma}A. Sequence analysis of the tsA12 S2 gene showed a single alteration, a cytosine-to-uracil transition, at nucleotide position 488. This alteration leads to a predicted amino acid change from proline to leucine at amino acid position 158 in the {sigma}A protein. An analysis of the core crystal structure of the closely related mammalian reovirus suggested that the Leu158 substitution in ARV {sigma}A lies directly under the outer face of the {sigma}A protein. This may cause a perturbation in {sigma}A such that outer capsid proteins are incapable of condensing onto nascent cores. Thus, the ARV tsA12 mutant represents a novel assembly-defective orthoreovirus clone that may prove useful for delineating virus assembly.

* Corresponding author. Mailing address: Department of Medical Microbiology and Infectious Diseases, University of Manitoba, Winnipeg, Manitoba, Canada R3E 0W3. Phone: (204) 789-3309. Fax: (204) 789-3926. E-mail: kcoombs{at}ms.umanitoba.ca.

Journal of Virology, October 2004, p. 11142-11151, Vol. 78, No. 20
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.20.11142-11151.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Roner, M. R., Steele, B. G. (2007). Features of the mammalian orthoreovirus 3 Dearing l1 single-stranded RNA that direct packaging and serotype restriction. J. Gen. Virol. 88: 3401-3412 [Abstract] [Full Text]  


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