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Norovirus RNA-dependent RNA polymerase is phosphorylated by an important survival kinase, Akt.

Abstract
Viruses commonly use host cell survival mechanisms to their own advantage. We show that Akt, an important signaling kinase involved in cell survival, phosphorylates the RNA-dependent RNA polymerase (RdRp) from norovirus, the major cause of gastroenteritis outbreaks worldwide. The Akt phosphorylation of RdRp appears to be a feature unique to the more prevalent norovirus genotypes such as GII.4 and GII.b. This phosphorylation event occurs at a residue (Thr33) located at the interface where the RdRp finger and thumb domains interact and decreases de novo activity of the polymerase. This finding provides fresh insights into virus-host cell interactions.
AuthorsJohn-Sebastian Eden, Laura J Sharpe, Peter A White, Andrew J Brown
JournalJournal of virology (J Virol) Vol. 85 Issue 20 Pg. 10894-8 (Oct 2011) ISSN: 1098-5514 [Electronic] United States
PMID21849454 (Publication Type: Journal Article)
Chemical References
  • Threonine
  • Oncogene Protein v-akt
  • RNA-Dependent RNA Polymerase
Topics
  • Host-Pathogen Interactions
  • Humans
  • Kinetics
  • Models, Molecular
  • Norovirus (physiology)
  • Oncogene Protein v-akt (metabolism)
  • Phosphorylation
  • RNA-Dependent RNA Polymerase (metabolism)
  • Threonine (metabolism)

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