Investigation of outer membrane protein recognition mechniams by human pathgen recognition receptors
Project/Area Number |
16K18506
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Structural biochemistry
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Research Institution | High Energy Accelerator Research Organization |
Principal Investigator |
Tanabe Mikio 大学共同利用機関法人高エネルギー加速器研究機構, 物質構造科学研究所, 特任准教授 (00716871)
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Research Collaborator |
STEINAM Claudia Georg-August-University Göttingen, Göttingen Graduate School for Neurosciences
Ulrich Zachariae University of Dundee, School of Life
Bahrmann Elmar Max plunck Society, Research Cenger Caesar
Paola Massari Tufts University, School of Medicine
Paola Stefanelli Istituto Superiore Di Sanità Department of Infectious, Parasitic&Immuno-Mediated Diseases
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Project Period (FY) |
2016-04-01 – 2018-03-31
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Project Status |
Completed (Fiscal Year 2017)
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Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2017: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2016: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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Keywords | 外膜タンパク質 / ヒト異物認識受容体 / X線結晶構造 / 感染症 / 薬剤耐性 / 抗生物質 / 物質輸送 / 生化学 / 自然免疫 / 膜タンパク質 / タンパク複合体 |
Outline of Final Research Achievements |
Porin is a β-barrel fold structure,, located in the outer membrane of Gram-negative bacteria, and responsible for which not only transports substrates essential for the biological activity of bacteria but also induces immunity via the foreign foreign body recognition receptor Toll-like receptor (TLR) Also play an important role. This research aimed at elucidating the role of the recognition mechanism of porins by TLR, and 2) the role of the porins themselves in the microbial cells, using biochemical techniques. 1), Porin from N.meningitidis, and the extracellular domain of TLR2 were purified and their complex formation were biochemically analyzed. 2), structural analysis of meningococcal porin, simulation of electrophysiology and molecular dynamics, and clarified substrate transport mechanism of β-lactam antibiotics.
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Report
(3 results)
Research Products
(9 results)