期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 115, 期 2, 页码 409-414出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1719369115
关键词
alpha-synuclein; eurodegeneration; proteinopathy; strains; synucleinopathies
资金
- NIH [AG002132, AG031220, AG005134]
- Dana Foundation
- Glenn Foundation
- Sherman Fairchild Foundation
- Henry M. Jackson Foundation
- Daiichi Sankyo
- Mary Jane Brinton Fund
In the neurodegenerative disease multiple system atrophy (MSA), alpha-synudein misfolds into a self-templating conformation to become a prion. To compare the biological activity of alpha-synudein prions in MSA and Parkinson's disease (PD), we developed nine alpha-synudein-YFP cell lines expressing point mutations responsible for inherited PD. MSA prions robustly infected wild-type, A30P, and A53T alpha-synudein-YFP cells, but they were unable to replicate in cells expressing the E46K mutation. Coexpression of the A53T and E46K mutations was unable to rescue MSA prion infection in vitro, establishing that MSA alpha-synudein prions are conformationally distinct from the misfolded alpha-synudein in PD patients. This observation may have profound implications for developing treatments for neurodegenerative diseases.
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