# |
PMID |
Sentence |
1 |
18534979
|
Mechanism of influenza A virus NS1 protein interaction with the p85beta, but not the p85alpha, subunit of phosphatidylinositol 3-kinase (PI3K) and up-regulation of PI3K activity.
|
2 |
18534979
|
Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by binding influenza A virus NS1 protein to the p85beta regulatory subunit of PI3K.
|
3 |
18534979
|
In this study, we report that NS1 binds to the inter-SH2 (iSH2) domain of p85beta.
|
4 |
18534979
|
Mutational analyses on p85beta iSH2 domain defined that Val-573 is the critical amino acid (AA) that mediates NS1 and p85beta interaction.
|
5 |
18534979
|
In reciprocal gain of function experiments with p85alpha, we demonstrated that mutation to Val at Met-582 leads to NS1 binding and increased PI3K activity.
|
6 |
18534979
|
Molecular modeling based on our experimental results suggested that, in addition to the interaction interface between the NS1 SH3 binding motif 1 (AA 164-167) and p85beta Val-573, AA 137-142 in NS1 might interact with p85beta.
|
7 |
18534979
|
Indeed, mutations of AA 141 and 142 in NS1 disrupted the interaction between NS1 and p85beta.
|
8 |
18534979
|
In contrast, in the mutant virus-infected cells containing mutant NS1 unable to interact with p85beta, the p85beta-associated PI3K activity up-regulation was not seen, suggesting that PI3K up-regulation is dependent upon the interaction between NS1 and p85beta.
|
9 |
18534979
|
Competition experiments and the immunoprecipitation studies demonstrated that NS1, p85beta, and p110 form a complex in cells.
|
10 |
18534979
|
Finally, the mechanism by which binding of NS1 to p85beta regulates PI3K activity was discussed based on a predicted structural model of NS1-p85-p110 complex.
|
11 |
19523910
|
The virus was partially attenuated at passage 40 (P40) and P70, and was fully attenuated at P110.
|
12 |
19523910
|
It lost immunogenicity and kidney tropism at P110 and P70, respectively.
|
13 |
19523910
|
Other substitutions that occurred between P70 and P110, however, were found only in some subpopulations of the virus passages.
|
14 |
19523910
|
A 109-bp deletion in the 3'-UTR was observed in most subpopulations of P70 and P110, and might be related to virus replication, transcription and pathogenicity.
|
15 |
19523910
|
The virus was partially attenuated at passage 40 (P40) and P70, and was fully attenuated at P110.
|
16 |
19523910
|
It lost immunogenicity and kidney tropism at P110 and P70, respectively.
|
17 |
19523910
|
Other substitutions that occurred between P70 and P110, however, were found only in some subpopulations of the virus passages.
|
18 |
19523910
|
A 109-bp deletion in the 3'-UTR was observed in most subpopulations of P70 and P110, and might be related to virus replication, transcription and pathogenicity.
|
19 |
19523910
|
The virus was partially attenuated at passage 40 (P40) and P70, and was fully attenuated at P110.
|
20 |
19523910
|
It lost immunogenicity and kidney tropism at P110 and P70, respectively.
|
21 |
19523910
|
Other substitutions that occurred between P70 and P110, however, were found only in some subpopulations of the virus passages.
|
22 |
19523910
|
A 109-bp deletion in the 3'-UTR was observed in most subpopulations of P70 and P110, and might be related to virus replication, transcription and pathogenicity.
|