期刊
PRION
卷 13, 期 1, 页码 46-52出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/19336896.2019.1569450
关键词
PrPSc structure; PrPSc syalilation; 4-rung beta-solenoid; PIRIBS; PrP23-144 infectious amyloid; cryo-electron microscopy; solid state NMR; Prion2018
资金
- Alberta Prion Research Institute [201600029]
- Intramural Research Program of the NIAID
- National Institute of Health [R01 NS045585, P01 AI106705, R01 NS083687, R01 NS103848]
- Spanish Ministry of Economy and Competitiveness [BFU2013-48436-C2-1-P, BFU2017-86692-P]
- Spanish Ministry of Science, Innovation and Universities [BFU2013-48436-C2-1-P, BFU2017-86692-P]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [ZIAAI000580] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R01NS045585] Funding Source: NIH RePORTER
Understanding the structure of PrPSc is without doubt a sine qua non to understand not only PrPSc propagation, but also critical features of that process such as the strain phenomenon and transmission barriers. While elucidation of the PrPSc structure has been full of difficulties, we now have a large amount of structural information that allows us to begin to understand it. This commentary article summarizes a round table that took place within the Prion 2018 meeting held in Santiago de Compostela to discuss the state of the art in this matter. Two alternative models of PrPSc exist: the PIRIBS and the 4-rung beta-solenoid models. Both of them have relevant features. The 4-rung beta-solenoid model agrees with experimental constraints of brain derived PrPSc obtained from cryo-EM and X-ray fiber diffraction studies. Furthermore, it allows facile accommodation of the bulky glycans that decorate brain-derived PrPSc. On the other hand, the infectious PrP23-144 amyloid exhibits a PIRIBS architecture. Perhaps, both types of structure co-exist.
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