PMID: 9658080Jul 11, 1998Paper

Analysis of rotavirus nonstructural protein NSP5 phosphorylation

Journal of Virology
J BlackhallG Magnusson

Abstract

The rotavirus nonstructural phosphoprotein NSP5 is encoded by a gene in RNA segment 11. Immunofluorescence analysis of fixed cells showed that NSP5 polypeptides remained confined to viroplasms even at a late stage when provirions migrated from these structures. When NSP5 was expressed in COS-7 cells in the absence of other viral proteins, it was uniformly distributed in the cytoplasm. Under these conditions, the 26-kDa polypeptide predominated. In the presence of the protein phosphatase inhibitor okadaic acid, the highly phosphorylated 28- and 32- to 35-kDa polypeptides were formed. Also, the fully phosphorylated protein had a homogeneous cytoplasmic distribution in transfected cells. In rotavirus SA11-infected cells, NSP5 synthesis was detectable at 2 h postinfection. However, the newly formed 26-kDa NSP5 was not converted to the 28- to 35-kDa forms until approximately 2 h later. Also, the protein kinase activity of isolated NSP5 was not detectable until the 28- and 30- to 35-kDa NSP5 forms had been formed. NSP5 immunoprecipitated from extracts of transfected COS-7 cells was active in autophosphorylation in vitro, demonstrating that other viral proteins were not required for this function. Treatment of NSP5-expressing cells wi...Continue Reading

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Citations

May 26, 2005·The Journal of General Virology·Tomás LópezCarlos F Arias
Nov 3, 2004·Proceedings of the National Academy of Sciences of the United States of America·Catherine EichwaldOscar R Burrone
Mar 3, 2004·The Journal of General Virology·Catherine EichwaldOscar R Burrone
Jul 29, 2006·Journal of Virology·Michela Campagna, Oscar R Burrone

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