The prion 2018 round tables (I): the structure of PrPSc.
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 β-solenoid models. Both of them have relevant features. The 4-rung β-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.
['Baskakov|Ilia V|IV|', 'Caughey|Byron|B|', 'Requena|Jesús R|JR|', 'Sevillano|Alejandro M|AM|', 'Surewicz|Witold K|WK|', 'Wille|Holger|H|']
D000682:Amyloid D000818:Animals D006031:Glycosylation D006801:Humans D051379:Mice D008954:Models, Biological D008958:Models, Molecular D018620:PrPSc Proteins
PIRIBS 4-rung β-solenoid PrP structure PrP syalilation PrP23-144 infectious amyloid Prion2018 cryo-electron microscopy solid state NMR