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. 2019 Dec 18;139(3):503–526. doi: 10.1007/s00401-019-02114-9

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© The Author(s) 2019

Open AccessThis 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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Fig. 2 — Soluble aggregates of Aβ, α-Synuclein and Tau bind to the N-terminus of PrP. a–c Binding of Aβ (a), αSyn (b) and tau (c) monomers, soluble aggregates and fibrils to immobilized PrP_23–231 was assessed using an ELISA-like microtiter plate assay. Data shown are the mean ± SD from a single experiment, whereas inset EC_50s are from at least four independent experiments. d–f Binding of soluble protein aggregates to immobilized PrP_23–231 can be inhibited by anti-PrP monoclonal antibodies (mAbs) to Sites I (MI-0131) and II (ICSM35), but not a nonspecific mAb (46–4). Data shown are the mean ± SD from a single experiment, whereas inset IC_50s are from at least four independent experiments. g–i To determine the regions of PrP involved in binding soluble protein aggregates, PrP_23–231, PrP_91–231, and PrP_119–231 were immobilized and binding of SBAs (g), SAAs (h) and STAs (i) measured. Data shown are the mean ± SD from a single experiment, whereas inset EC_50s are from at least 4 independent experiments