Thermostability as a highly dependent prion strain feature

Scientific Reports
Alba Marín-MorenoJuan María Torres

Abstract

Prion diseases are caused by the conversion of physiological PrPC into the pathogenic misfolded protein PrPSc, conferring new properties to PrPSc that vary upon prion strains. In this work, we analyze the thermostability of three prion strains (BSE, RML and 22L) that were heated at 98 °C for 2 hours. PrPSc resistance to proteinase K (PrPres), residual infectivity by mouse bioassay and in vitro templating activity by protein misfolding cyclic amplification (PMCA) were studied. Heated strains showed a huge loss of PrPres and a radically different infectivity loss: RML was the most thermolabile strain (6 to 7 log10 infectivity loss), followed by 22L (5 log10) while BSE was the most thermostable strain with low or null infectivity reduction showing a clear dissociation between PrPres and infectivity. These results indicate that thermostability is a strain-specific feature, measurable by PMCA and mouse bioassay, and a great tool to distinguish prion strains.

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Citations

Oct 11, 2019·MSphere·Sara A M HolecJason C Bartz
Dec 19, 2020·Frontiers in Bioengineering and Biotechnology·Mohammed MoudjouAngélique Igel-Egalon
Apr 27, 2021·Acta Neuropathologica·Jason C Bartz
Aug 21, 2021·Current Opinion in Neurobiology·Manfredi Carta, Adriano Aguzzi

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Methods Mentioned

BETA
enzyme-linked immunosorbent assay
electrophoresis
PCR

Software Mentioned

ImageLab

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