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Journal of Virology, July 2006, p. 6917-6925, Vol. 80, No. 14
0022-538X/06/$08.00+0     doi:10.1128/JVI.01152-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Analyses of Phosphorylation Events in the Rubella Virus Capsid Protein: Role in Early Replication Events

LokMan J. Law,1,{dagger} Carolina S. Ilkow,1,{dagger} Wen-Pin Tzeng,2,{dagger} Matthew Rawluk,3 David T. Stuart,3 Teryl K. Frey,2 and Tom C. Hobman1,4*

Departments of Cell Biology,1 Biochemistry,3 Medical Microbiology and Immunology, 5-14 Medical Sciences Building, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada,4 Department of Biology, Georgia State University, Atlanta, Georgia 30302-40102

Received 6 June 2005/ Accepted 26 April 2006

The Rubella virus capsid protein is phosphorylated prior to virus assembly. Our previous data are consistent with a model in which dynamic phosphorylation of the capsid regulates its RNA binding activity and, in turn, nucleocapsid assembly. In the present study, the process of capsid phosphorylation was examined in further detail. We show that phosphorylation of serine 46 in the RNA binding region of the capsid is required to trigger phosphorylation of additional amino acid residues that include threonine 47. This residue likely plays a direct role in regulating the binding of genomic RNA to the capsid. We also provide evidence which suggests that the capsid is dephosphorylated prior to or during virus budding. Finally, whereas the phosphorylation state of the capsid does not directly influence the rate of synthesis of viral RNA and proteins or the assembly and secretion of virions, the presence of phosphate on the capsid is critical for early events in virus replication, most likely the uncoating of virions and/or disassembly of nucleocapsids.

* Corresponding author. Mailing address: Department of Cell Biology, 5-14 Medical Sciences Building, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada. Phone and fax: (780) 492-0450. E-mail: tom.hobman{at}ualberta.ca.

{dagger} These authors contributed equally to this work.

Journal of Virology, July 2006, p. 6917-6925, Vol. 80, No. 14
0022-538X/06/$08.00+0     doi:10.1128/JVI.01152-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Wu, C.-H., Yeh, S.-H., Tsay, Y.-G., Shieh, Y.-H., Kao, C.-L., Chen, Y.-S., Wang, S.-H., Kuo, T.-J., Chen, D.-S., Chen, P.-J. (2009). Glycogen Synthase Kinase-3 Regulates the Phosphorylation of Severe Acute Respiratory Syndrome Coronavirus Nucleocapsid Protein and Viral Replication. J. Biol. Chem. 284: 5229-5239 [Abstract] [Full Text]  
  • Ilkow, C. S., Mancinelli, V., Beatch, M. D., Hobman, T. C. (2008). Rubella Virus Capsid Protein Interacts with Poly(A)-Binding Protein and Inhibits Translation. J. Virol. 82: 4284-4294 [Abstract] [Full Text]  


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