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. 2020 Jul 9;3:365. doi: 10.1038/s42003-020-1085-z

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© The Author(s) 2020

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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Fig. 1 — a Scheme of αSynO-PrP^C signaling. αSynO binds to membrane-anchored PrP^C and activates Fyn kinase via metabotropic glutamate receptor 5 (mGluR5), leading to phosphorylation of N-methyl-d-aspartate receptors (NMDAR) and finally to elevated intracellular calcium levels⁹. The naturally produced huPrP fragment N1 (residues 23−110/111) might prevent αSynO toxicity, analogous to its effect on AβO toxicity^17,29–31. b Full-length huPrP(23−230) and seven fragments were investigated. OR octarepeat region. Orange, region needed for AβO binding^15–19 which is almost the same region described to be necessary for αSynO binding⁹. huPrP(23−230), huPrP(90−230), and huPrP(121−230) contain a disulfide bond between Cys179 and Cys214.