Molecular analysis of immune evasion mechanisms by mycobacteria

2014 Fiscal Year Final Research Report

• Project/Area Number: 25870796
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Immunology; Biological pharmacy
• Research Institution: Hoshi University
• Principal Investigator: OKU Teruaki 星薬科大学, 薬学部, 助教 (20409361)
• Project Period (FY): 2013-04-01 – 2015-03-31
• Keywords: Coronin / リン酸化 / 結核 / 細胞内寄生 / LpdC / PKC / ファゴソーム

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

Free Research Field

生化学