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Journal of Virology, August 2006, p. 7729-7739, Vol. 80, No. 15
0022-538X/06/$08.00+0     doi:10.1128/JVI.00425-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Ribosomal Protein S6 Associates with Alphavirus Nonstructural Protein 2 and Mediates Expression from Alphavirus Messages

Stephanie A. Montgomery,1,2* Peter Berglund,3 Clayton W. Beard,1,2 and Robert E. Johnston1,2

Department of Microbiology and Immunology,1 Carolina Vaccine Institute, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599,2 Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 208923

Received 28 February 2006/ Accepted 9 May 2006

Although alphaviruses dramatically alter cellular function within hours of infection, interactions between alphaviruses and specific host cellular proteins are poorly understood. Although the alphavirus nonstructural protein 2 (nsP2) is an essential component of the viral replication complex, it also has critical auxiliary functions that determine the outcome of infection in the host. To gain a better understanding of nsP2 function, we sought to identify cellular proteins with which Venezuelan equine encephalitis virus nsP2 interacted. We demonstrate here that nsP2 associates with ribosomal protein S6 (RpS6) and that nsP2 is present in the ribosome-containing fractions of a polysome gradient, suggesting that nsP2 associates with RpS6 in the context of the whole ribosome. This result was noteworthy, since viral replicase proteins have seldom been described in direct association with components of the ribosome. The association of RpS6 with nsP2 was detected throughout the course of infection, and neither the synthesis of the viral structural proteins nor the presence of the other nonstructural proteins was required for RpS6 interaction with nsP2. nsP1 also was associated with RpS6, but other nonstructural proteins were not. RpS6 phosphorylation was dramatically diminished within hours after infection with alphaviruses. Furthermore, a reduction in the level of RpS6 protein expression led to diminished expression from alphavirus subgenomic messages, whereas no dramatic diminution in cellular translation was observed. Taken together, these data suggest that alphaviruses alter the ribosome during infection and that this alteration may contribute to differential translation of host and viral messages.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, CB 7292, Mary Ellen Jones Bldg., University of North Carolina at Chapel Hill, Chapel Hill, NC 27599. Phone: (919) 966-4026. Fax: (919) 843-6924. E-mail: smontgo{at}med.unc.edu.

Journal of Virology, August 2006, p. 7729-7739, Vol. 80, No. 15
0022-538X/06/$08.00+0     doi:10.1128/JVI.00425-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gorchakov, R., Frolova, E., Sawicki, S., Atasheva, S., Sawicki, D., Frolov, I. (2008). A New Role for ns Polyprotein Cleavage in Sindbis Virus Replication. J. Virol. 82: 6218-6231 [Abstract] [Full Text]  
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