| Project Area | Matrix of Infection Phenomena |
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| Project/Area Number |
18073011
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| Research Category |
Grant-in-Aid for Scientific Research on Priority Areas
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| Allocation Type | Single-year Grants |
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| Review Section |
Biological Sciences
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| Research Institution | Osaka University |
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Principal Investigator |
KAWABATA Shigetada Osaka University, 大学院・歯学研究科, 教授 (50273694)
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| Co-Investigator(Kenkyū-buntansha) |
TERAO Yutaka 大阪大学, 大学院・歯学研究科, 准教授 (50397717)
NAKATA Masanobu 大阪大学, 大学院・歯学研究科, 助教 (90444497)
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| Project Period (FY) |
2006 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥93,000,000 (Direct Cost: ¥93,000,000)
Fiscal Year 2010: ¥18,600,000 (Direct Cost: ¥18,600,000)
Fiscal Year 2009: ¥18,600,000 (Direct Cost: ¥18,600,000)
Fiscal Year 2008: ¥18,600,000 (Direct Cost: ¥18,600,000)
Fiscal Year 2007: ¥18,600,000 (Direct Cost: ¥18,600,000)
Fiscal Year 2006: ¥18,600,000 (Direct Cost: ¥18,600,000)
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| Keywords | レンサ球菌 / 組織侵入 / 増殖 / タンパク質 / 病原因子 / 感染症 / 細菌 / 微生物 / 免疫学 / バイオ関連機器 / SpeB / A群レンサ球菌 / 自然免疫 / 回避機構 / 補体 / C3b / C5a / システインプロテアーゼ |
|---|
| Research Abstract |
Streptococcus pyogenes causes pharyngitis, sepsis, and rheumatic fever. Cell-associated streptococcal C5a peptidase (ScpA) protects S. pyogenes from phagocytosis and has been suggested to interrupt host defenses by enzymatically cleaving complement C5a, a major factor in the accumulation of neutrophils at sites of infection. How S. pyogenes recognizes and binds to C5a, however, is unclear. We detected a C5a-binding protein in 8 M urea extracts of S. pyogenes by ligand blotting using biotinylated C5a. Searching of genome databases showed that the C5a-binding protein is identical to the streptococcal plasmin receptor (Plr), also known as streptococcal surface dehydrogenase (SDH) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). In the present study, we identified a novel function of this multifunctional protein. We examined whether the streptococcal Plr/SDH/GAPDH inhibits the biological effects of C5a on human neutrophils. Together, these results indicate that the multifunctional protein Plr/SDH/GAPDH has additional functions that help S. pyogenes escape detection by the host immune system.
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