Molecular mechanism behind rotavirus NSP1-mediated PI3 kinase activation: interaction between NSP1 and the p85 subunit of PI3 kinase

J Virol. 2013 Feb;87(4):2358-62. doi: 10.1128/JVI.02479-12. Epub 2012 Dec 5.


Our previous study had reported on the interaction of rotavirus NSP1 with cellular phosphoinositide 3-kinase (PI3K) during activation of the PI3K pathway (P. Bagchi et al., J. Virol. 84:6834-6845, 2010). In this study, we have analyzed the molecular mechanism behind this interaction. Results showed that this interaction is direct and that both α and β isomers of the PI3K regulatory subunit p85 and full-length NSP1 are important for this interaction, which results in efficient activation of the PI3K/Akt pathway during rotavirus infection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line
  • Humans
  • Phosphatidylinositol 3-Kinases / metabolism*
  • Protein Binding
  • Protein Interaction Mapping*
  • Rotavirus / physiology*
  • Two-Hybrid System Techniques
  • Viral Nonstructural Proteins / metabolism*


  • Viral Nonstructural Proteins
  • nsp1 protein, Rotavirus