Molecular analysis of immune evasion mechanisms by mycobacteria
| Project/Area Number |
25870796
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Immunology
Biological pharmacy
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| Research Institution | Hoshi University |
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Principal Investigator |
OKU Teruaki 星薬科大学, 薬学部, 助教 (20409361)
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2014: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | Coronin / リン酸化 / 結核 / 細胞内寄生 / LpdC / PKC / ファゴソーム / Coronin-1 / アクチン結合タンパク質 / 食作用 / 結核菌 / 貪食機構 |
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| Outline of Final Research Achievements |
In this study, we examined which PKC isoforms have influence on phosphorylation of p57/coronin-1 at Thr-412 using isotype-specific PKC inhibitors and short interfering RNAs (siRNAs). The results indicate that p57/coronin-1 at Thr-412 is phosphorylated by PKCalpha. Next we prepared mutant of p57/coronin-1 at Thr-412, an Asp mutant (T412D), that mimic the phosphorylated form. To examine whether Thr-412 phosphorylation affects the interaction of p57/coronin-1 with mycobacterial lipoamide dehydrogenase C (LpdC), we conducted co-purification of LpdC with p57/coronin-1 (wild-type or T412D mutant). We observed the LpdC was associated with wild-type of p57/coronin-1 but not with T412D mutant. These results suggest that the mechanism of immune evasion by mycobacteria is inhibition of phosphorylation with PKCalpha of p57/coronin-1 at Thr-412 by binding with LpdC
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Report
(3 results)
Research Products
(4 results)
