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Hyperphosphorylation of the Rotavirus NSP5 Protein Is Independent of Serine 67 or NSP2, and the Intrinsic Insolubility of NSP5 Is Regulated by Cellular Phosphatases

The NSP5 protein is required for viroplasm formation during rotavirus infection and is hyperphosphorylated into 32- to 35-kDa isoforms. Earlier studies reported that NSP5 is not hyperphosphorylated without NSP2 coexpression or deleting the NSP5 N terminus and that serine 67 is essential for NSP5 hyp...

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Detalles Bibliográficos
Main Authors: Sen, Adrish, Agresti, Darin, Mackow, Erich R.
Formato: Artigo
Idioma:Inglês
Publicado: American Society for Microbiology 2006
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC1367154/
https://ncbi.nlm.nih.gov/pubmed/16439537
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JVI.80.4.1807-1816.2006
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