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Researchers Elucidate the Molecular Mechanism of the Diverse Prion Strains
Update time: 2021-09-10
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Recently, a research paper titled “Genetic prion disease–related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM” was published on the Science Advances journal by Prof. LIU Cong from the Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, in collaboration with Prof. LIANG Yi from Wuhan University.
Prion diseases are infectious, fatal neurodegenerative diseases primarily caused by the conformational conversion of prion protein (PrP) from its cellular form (PrPC) into a protease-resistant, aggregated form (PrPSc). Forty-two different mutations in the PrP gene (PRNP) were identified to cause a variety of genetic prion diseases, including genetic Creutzfeldt-Jakob disease (CJD), Gerstmann-Str?ussler-Scheinker disease, and fatal familial insomnia. However, the roles of disease-related mutations play in prion fibril structure and the molecular mechanism of the diverse prion strains are still unknow.
In this paper, researchers obtained homogeneous amyloid fibrils in vitro from recombinant, full-length human E196K PrP and determined the near atomic structure by using cryo-EM. The results showed that the E196K mutation disrupts key interactions in the wild-type PrP fibril, forming an amyloid fibril with a conformation distinct from the wild-type PrP fibril. This study elucidates the molecular mechanism of the diverse prion strains and sheds light on the development of new strategies and targets for diagnosis and treatment of diseases.

LIU Cong Ph.D. Professor
Tel: 021-68582528
Email: liulab@sioc.ac.cn
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