| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2019: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2018: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2017: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Outline of Final Research Achievements |
To evade host immunity, many pathogenic viruses inactivate host JAK-STAT pathways using diverse strategies. Measles virus utilizes P and V proteins to counteract this signaling pathway. Our data indicate that interactions between the C-terminal domain (CTD) of V and STAT2 is one order of magnitude stronger than that of the N-terminal region of V and STAT1. We also clarified those interactions are completely independent each other in solution. These results provide a novel model that MeV-V can not only inhibit the STAT2/IRF9 interaction but also disrupt pre-assembled ISGF3. For CTD of rabies virus P protein, we analyze the structures of the CTD of P of Duvenhage and of a distinct rabies virus strain to gain further insight on the nature and potential function of the hydrophobic surface. Molecular contacts suggest that the hydrophobic patch is important to intermolecular interactions with other proteins, which differ between the lyssavirus species.
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