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. 2020 Dec 1;8:591024. doi: 10.3389/fbioe.2020.591024

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Copyright © 2020 Moudjou, Castille, Passet, Herzog, Reine, Vilotte, Rezaei, Béringue and Igel-Egalon.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Scheme summarizing the principles of the RT-QuIC and PMCA assays. (A) RT-QuIC is based on the polymerization of recombinant PrP protein by prions in the test sample. During iterative cycles of shaking and quiescent incubation, polymerization is monitored in real-time by the increase in Thioflavin T fluorescence. (B) PMCA is based on the bona fide conversion of brain PrP^C by prions in the test sample. Conversion is favored by iterative cycles of quiescent incubation and sonication. At the end of the reaction, the presence of abnormal PrP^Sc is analyzed by proteinase K digestion and western blot. In both methods, prion seeding activity in the test sample can be quantified by limiting dilution titration.