Molecular Mechanism behind Rotavirus NSP1-Mediated PI3 Kinase Activation: Interaction between NSP1 and the p85 Subunit of PI3 Kinase
Molecular Mechanism behind Rotavirus NSP1-Mediated PI3 Kinase Activation: Interaction between NSP1 and the p85 Subunit of PI3 Kinase
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DOI：
10.1128/jvi.02479-12
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发表时间：
2013-02-01
影响因子：
5.4
通讯作者：
Chawla-Sarkar, Mamta
中科院分区：
文献类型：
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作者：
Bagchi, Parikshit;Nandi, Satabdi;Chawla-Sarkar, Mamta
我们之前的研究已经报道了轮状病毒NSP1与细胞磷脂酰肌醇3-激酶(PI3K)在PI3K途径激活过程中的相互作用(P.Bagchi等人，J.Virol)。84：6834-6845,2010)。在这项研究中，我们分析了这种相互作用背后的分子机制。结果表明，这种相互作用是直接的，并且PI3K调节亚单位P85的α和β异构体和全长NSP1对这种相互作用都是重要的，这导致了轮状病毒感染过程中PI3K/Akt通路的有效激活。
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 alpha and beta 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.