{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T03:03:33Z","timestamp":1787022213690,"version":"build-2736575974"},"reference-count":103,"publisher":"Public Library of Science (PLoS)","issue":"9","license":[{"start":{"date-parts":[[2024,9,12]],"date-time":"2024-09-12T00:00:00Z","timestamp":1726099200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000096","name":"Scottish Rite Charitable Foundation of Canada","doi-asserted-by":"publisher","award":["18119"],"award-info":[{"award-number":["18119"]}],"id":[{"id":"10.13039\/501100000096","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["PJT-169042"],"award-info":[{"award-number":["PJT-169042"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    The cellular prion protein, PrP\n                    <jats:sup>C<\/jats:sup>\n                    , has been postulated to function as a receptor for \u03b1-synuclein, potentially facilitating cell-to-cell spreading and\/or toxicity of \u03b1-synuclein aggregates in neurodegenerative disorders such as Parkinson\u2019s disease. Previously, we generated the \u201cSalt (S)\u201d and \u201cNo Salt (NS)\u201d strains of \u03b1-synuclein aggregates that cause distinct pathological phenotypes in M83 transgenic mice overexpressing A53T-mutant human \u03b1-synuclein. To test the hypothesis that PrP\n                    <jats:sup>C<\/jats:sup>\n                    facilitates the propagation of \u03b1-synuclein aggregates, we produced M83 mice that either express or do not express PrP\n                    <jats:sup>C<\/jats:sup>\n                    . Following intracerebral inoculation with the S or NS strain, the absence of PrP\n                    <jats:sup>C<\/jats:sup>\n                    in M83 mice did not prevent disease development and had minimal influence on \u03b1-synuclein strain-specified attributes such as the extent of cerebral \u03b1-synuclein deposition, selective targeting of specific brain regions and cell types, the morphology of induced \u03b1-synuclein deposits, and the structural fingerprints of protease-resistant \u03b1-synuclein aggregates. Likewise, there were no appreciable differences in disease manifestation between PrP\n                    <jats:sup>C<\/jats:sup>\n                    -expressing and PrP\n                    <jats:sup>C<\/jats:sup>\n                    -lacking M83 mice following intraperitoneal inoculation of the S strain. Interestingly, intraperitoneal inoculation with the NS strain resulted in two distinct disease phenotypes, indicative of \u03b1-synuclein strain evolution, but this was also independent of PrP\n                    <jats:sup>C<\/jats:sup>\n                    expression. Overall, these results suggest that PrP\n                    <jats:sup>C<\/jats:sup>\n                    plays at most a minor role in the propagation, neuroinvasion, and evolution of \u03b1-synuclein strains in mice that express A53T-mutant human \u03b1-synuclein. Thus, other putative receptors or cell-to-cell propagation mechanisms may have a larger effect on the spread of \u03b1-synuclein aggregates during disease.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1012517","type":"journal-article","created":{"date-parts":[[2024,9,12]],"date-time":"2024-09-12T13:26:48Z","timestamp":1726147608000},"page":"e1012517","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":9,"title":["\u03b1-Synuclein strain propagation is independent of cellular prion protein expression in a transgenic synucleinopathy mouse model"],"prefix":"10.1371","volume":"20","author":[{"given":"Raphaella W. L.","family":"So","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Genki","family":"Amano","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erica","family":"Stuart","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aeen","family":"Ebrahim Amini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adriano","family":"Aguzzi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Graham L.","family":"Collingridge","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2604-2925","authenticated-orcid":true,"given":"Joel C.","family":"Watts","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2024,9,12]]},"reference":[{"issue":"6645","key":"ppat.1012517.ref001","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/42166","article-title":"Alpha-synuclein in Lewy bodies","volume":"388","author":"MG Spillantini","year":"1997","journal-title":"Nature"},{"key":"ppat.1012517.ref002","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1111\/j.1749-6632.2000.tb06900.x","article-title":"The alpha-synucleinopathies: Parkinson\u2019s disease, dementia with Lewy bodies, and multiple system atrophy","volume":"920","author":"MG Spillantini","year":"2000","journal-title":"Ann N Y Acad Sci"},{"issue":"5999","key":"ppat.1012517.ref003","doi-asserted-by":"crossref","first-page":"1663","DOI":"10.1126\/science.1195227","article-title":"Alpha-synuclein promotes SNARE-complex assembly in vivo and in 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