title: Molecular mechanism behind rotavirus NSP1-mediated PI3 kinase activation: interaction between NSP1 and the p85 subunit of PI3 kinase.
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.
authors.affiliation: Division of Virology, National Institute of Cholera and Enteric Diseases, Beliaghata, Kolkata, India.
authors.forename: Parikshit
authors.initials: P
authors.lastname: Bagchi
authors.forename: Satabdi
authors.initials: S
authors.lastname: Nandi
authors.forename: Mukti Kant
authors.initials: MK
authors.lastname: Nayak
authors.forename: Mamta
authors.initials: M
authors.lastname: Chawla-Sarkar
mesh_terms: D002460:Cell Line; D006801:Humans; D019869:Phosphatidylinositol 3-Kinases / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping; D012401:Rotavirus / Q000502:physiology*; D020798:Two-Hybrid System Techniques; D017361:Viral Nonstructural Proteins / Q000378:metabolism*
chemical_list: D019869:Phosphatidylinositol 3-Kinases; D017361:Viral Nonstructural Proteins; C104282:nsp1 protein, Rotavirus