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. 2017 Aug 30;7:10050. doi: 10.1038/s41598-017-10236-x

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Clearance of PrP^Sc from RML prion-infected cells in the presence of α-Syn amyloids. (a) PrP^Sc levels in ScN2a cells were measured by immunoblotting after four days of culture in the presence of different α-Syn preparations (monomeric and fibrillar α-Syn). (b) Western blot analysis of PK-resistant PrP^Sc in ScN2a cell lysates after treatment with monomeric α-Syn (grey arrow) or different α-Syn amyloids (short non-sonicated fibrils, red arrow; short sonicated fibrils, blue arrow; long non-sonicated fibrils, green arrow; long sonicated fibrils, magenta arrow) over four serial passages. (c) Quantification of three independent experiments. The values are shown as a percentage of PK-resistant form relative to total PrP/β-actin. β-Actin is a loading control. Data are represented as mean ± SD. Data were evaluated by unpaired Student’s t-test. Statistical analysis is indicated as: *P < 0.05, **P < 0.01, ***P < 0.001.