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. 2021 May 12;11:10109. doi: 10.1038/s41598-021-89586-6

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© The Author(s) 2021

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Different biochemical properties of PrP^Sc in N2aC24(R1) cells from PrP^Sc in RML- and 22L-infected N2aC24 cells. (a) Western blotting of N2aC24(R1), RML-infected N2aC24Chm (Chm), and 22L-infected N2aC24L1-3 cells (L1-3) with 6D11 antibody after treatment with or without PK (20 μg/mg of proteins). PK-untreated 15 μg proteins from each cell lysate were used for detection of total PrP (Left panel) and PK-treated 30 μg proteins for PrP^Sc (Middle panel) Aliquots of the PK-treated samples were also treated with PNGase F before Western blotting (Right panel). β-actin was used as an internal control. (b) Ratio (%) of di-, mono-, and un-glycosylated PrP^Sc in the Middle panel of (a). (c) Western blotting (Left panels) of PrP^Sc and its signal intensities (Right panel, n = 3) in RML-infected N2aC24Chm (Chm, Upper panel), N2aC24(R1) (Middle panel), and 22L-infected N2aC24L1-3 cells (L1-3, Lower panel) with 6D11 antibody after treatment with different concentrations of GdnHCl. Full length blots of Western blot images are shown in Supplementary Fig. 11.