HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Campagna, M. Articles by Burrone, O. R. Search for Related Content PubMed PubMed Citation Articles by Campagna, M. Articles by Burrone, O. R. Agricola Articles by Campagna, M. Articles by Burrone, O. R.

Impaired hyperphosphorylation of rotavirus NSP5 in cells depleted of casein kinase 1 is associated with the formation of viroplasms with altered morphology and a moderate decrease in virus replication

¹ International Centre for Genetic Engineering and Biotechnology, Padriciano 99, 34011 Trieste, Italy
² Instituto de Ciencias Biomedicas, Programa de Biologia Celular y Molecular, Facultad de Medicina, Universidad de Chile, Independencia 1027, 8380453 Santiago, Chile

Correspondence
Oscar R. Burrone
burrone{at}icgeb.org

The rotavirus (RV) non-structural protein 5, NSP5, is encoded by the smallest of the 11 genomic segments and localizes in ‘viroplasms’, cytoplasmic inclusion bodies in which viral RNA replication and packaging take place. NSP5 is essential for the replicative cycle of the virus because, in its absence, viroplasms are not formed and viral RNA replication and transcription do not occur. NSP5 is produced early in infection and undergoes a complex hyperphosphorylation process, leading to the formation of proteins differing in electrophoretic mobility. The role of hyperphosphorylation of NSP5 in the replicative cycle of rotavirus is unknown. Previous in vitro studies have suggested that the cellular kinase CK1 is responsible for the NSP5 hyperphosphorylation process. Here it is shown, by means of specific RNA interference, that in vivo, CK1 is the enzyme that initiates phosphorylation of NSP5. Lack of NSP5 hyperphosphorylation affected neither its interaction with the virus VP1 and NSP2 proteins normally found in viroplasms, nor the production of viral proteins. In contrast, the morphology of viroplasms was altered markedly in cells in which CK1 was depleted and a moderate decrease in the production of double-stranded RNA and infectious virus was observed. These data show that CK1 is the kinase that phosphorylates NSP5 in virus-infected cells and contribute to further understanding of the role of NSP5 in RV infection.

This article has been cited by other articles:

				N. J. MacLaine, B. Oster, B. Bundgaard, J. A. Fraser, C. Buckner, P. A. Lazo, D. W. Meek, P. Hollsberg, and T. R. Hupp A Central Role for CK1 in Catalyzing Phosphorylation of the p53 Transactivation Domain at Serine 20 after HHV-6B Viral Infection J. Biol. Chem., October 17, 2008; 283(42): 28563 - 28573. [Abstract] [Full Text] [PDF]

				J. L. Zambrano, Y. Diaz, F. Pena, E. Vizzi, M.-C. Ruiz, F. Michelangeli, F. Liprandi, and J. E. Ludert Silencing of Rotavirus NSP4 or VP7 Expression Reduces Alterations in Ca2+ Homeostasis Induced by Infection of Cultured Cells J. Virol., June 15, 2008; 82(12): 5815 - 5824. [Abstract] [Full Text] [PDF]