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

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

Author information

1
Division of Virology, National Institute of Cholera and Enteric Diseases, Beliaghata, Kolkata, India.

Abstract

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.

PMID:
23221569
PMCID:
PMC3571490
DOI:
10.1128/JVI.02479-12
[Indexed for MEDLINE]
Free PMC Article

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