Thermostability as a highly dependent prion strain feature - INRAE - Institut national de recherche pour l’agriculture, l’alimentation et l’environnement
Article Dans Une Revue Scientific Reports Année : 2019

Thermostability as a highly dependent prion strain feature

Résumé

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 degrees 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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hal-02619920 , version 1 (25-05-2020)

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Alba Marin-Moreno, Patricia Aguilar-Calvo, Mohammed Moudjou, Juan Carlos Espinosa, Vincent Béringue, et al.. Thermostability as a highly dependent prion strain feature. Scientific Reports, 2019, 9 (1), ⟨10.1038/s41598-019-47781-6⟩. ⟨hal-02619920⟩
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