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2018 Fiscal Year Final Research Report

The elucidation of molecular basis of the diversity and transmissibility in abnormal prion protein formation

Research Project

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Project/Area Number 15H04269
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypeSingle-year Grants
Section一般
Research Field Nerve anatomy/Neuropathology
Research InstitutionUniversity of Miyazaki (2016-2018)
Nagasaki University (2015)

Principal Investigator

Atarashi Ryuichiro  宮崎大学, 医学部, 教授 (90452846)

Research Collaborator IMAMURA morikazu  
Project Period (FY) 2015-04-01 – 2019-03-31
Keywordsプリオン病 / プリオン株 / PrP
Outline of Final Research Achievements

Accumulating evidence suggests that the continuous conversion of normal form of prion protein (PrPC) into abnormal form of PrP (PrPSc) in affected hosts plays a central role of the pathogenesis of prion diseases. However, the molecular basis of the diversity and transmissibility in PrPSc formation has not been well understood. Using the protein misfolding cyclic amplification (PMCA) technique, we found that some cofactors such as heparin sulfate or its analog heparin greatly enhanced the formation of PrPSc in vitro. Furthermore, we developed an advanced PMCA system using E-coli derived recombinant PrP as a substrate. We currently examined the diversity and transmissibility of the advanced PMCA products.

Free Research Field

ウイルス学

Academic Significance and Societal Importance of the Research Achievements

補助的因子を加えた試験管内異常化反応法により、これまで効率の低かったプリオン株(非典型牛海綿状脳症や慢性消耗病等)の高効率な変換が可能となった。またその補助的因子を加えることにより、大腸菌由来リコンビナントPrP(recPrP)を反応基質とした試験管内PrP異常化反応系において、そのプリオン株特有の産物を生成させることが初めて可能となった。これらの結果は、プリオン病の病態機構の理解を大きく進展させたと考えている。

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Published: 2020-03-30  

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