{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T22:31:46Z","timestamp":1790202706834,"version":"4.1.0"},"update-to":[{"DOI":"10.1371\/journal.ppat.1013911","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2026,2,3]],"date-time":"2026-02-03T00:00:00Z","timestamp":1770076800000}}],"reference-count":60,"publisher":"Public Library of Science (PLoS)","issue":"1","license":[{"start":{"date-parts":[[2026,1,28]],"date-time":"2026-01-28T00:00:00Z","timestamp":1769558400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    The mechanism by which prions composed of PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    cause the neuropathological aberrations characteristic of prion diseases remains elusive. Previous studies have defined a synaptotoxic signaling pathway in which extracellular PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    stimulates NMDA receptor-mediated Ca\n                    <jats:sup>2+<\/jats:sup>\n                    influx, activation of p38 MAPK, and collapse of the actin cytoskeleton in dendritic spines, resulting in functional decrements in synaptic transmission. However, these studies did not determine whether synaptotoxic signaling is directly linked to conversion of cell-surface PrP\n                    <jats:sup>C<\/jats:sup>\n                    to PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    , or whether it can be initiated by extracellular PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    independently of PrP conversion. To address this question, we employed two different experimental strategies, both of which interfere with PrP\n                    <jats:sup>C<\/jats:sup>\n                    -PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    conversion: (1) neuronal expression of PrP\n                    <jats:sup>C<\/jats:sup>\n                    mutants that are locked in the PrP\n                    <jats:sup>C<\/jats:sup>\n                    conformation (G126V and V208M); and (2) application of extracellular PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    from a species (mouse or hamster) that is unable to convert neuronal PrP\n                    <jats:sup>C<\/jats:sup>\n                    of the other species. We first confirmed that both of these strategies resulted in impaired PrP\n                    <jats:sup>C<\/jats:sup>\n                    -PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    conversion in cultured N2a and CAD5 cell lines. To assay synaptotoxicity, we then used lentiviral transduction to express the PrP\n                    <jats:sup>C<\/jats:sup>\n                    variants in primary cultures of hippocampal neurons from PrP-null mice, and quantitated dendritic spine density after exposure to purified prions. Expression of G126V PrP completely prevented spine retraction in response to three different murine prion strains (RML, 22L, and ME7), while the effect of V208M PrP was strain-dependent, consistent with partial stabilization of PrP structure by this mutation. Expression of hamster PrP\n                    <jats:sup>C<\/jats:sup>\n                    or mouse PrP\n                    <jats:sup>C<\/jats:sup>\n                    greatly attenuated spine retraction in response to murine 22L and hamster 263K prions, respectively. These findings support a model in which newly formed PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    at the neuronal surface is required to initiate prion-mediated synaptotoxic signaling. This work also suggests use of the G126V mutation as part of a therapeutic strategy to reduce PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    conversion in prion diseases.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1013911","type":"journal-article","created":{"date-parts":[[2026,1,28]],"date-time":"2026-01-28T18:35:11Z","timestamp":1769625311000},"page":"e1013911","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":7,"title":["Membrane-anchored PrPSc is the trigger for prion synaptotoxicity"],"prefix":"10.1371","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4322-3880","authenticated-orcid":true,"given":"Jean R. P.","family":"Gatdula","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6029-511X","authenticated-orcid":true,"given":"Robert C. C.","family":"Mercer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jose Andres","family":"Alepuz Guillen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Janelle S.","family":"Vultaggio","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6985-5790","authenticated-orcid":true,"given":"David A.","family":"Harris","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2026,1,28]]},"reference":[{"issue":"23","key":"ppat.1013911.ref001","doi-asserted-by":"crossref","first-page":"13363","DOI":"10.1073\/pnas.95.23.13363","article-title":"Prions","volume":"95","author":"SB Prusiner","year":"1998","journal-title":"Proceedings of the National Academy of Sciences"},{"issue":"4542","key":"ppat.1013911.ref002","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1126\/science.6801762","article-title":"Novel proteinaceous infectious particles cause scrapie","volume":"216","author":"SB Prusiner","year":"1982","journal-title":"Science"},{"key":"ppat.1013911.ref003","first-page":"23","article-title":"Prion Diseases","author":"RCC Mercer","year":"2018","journal-title":"The Molecular and Cellular Basis of Neurodegenerative Diseases. Elsevier"},{"issue":"7","key":"ppat.1013911.ref004","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1007864","article-title":"Full atomistic model of prion structure and conversion","volume":"15","author":"G Spagnolli","year":"2019","journal-title":"PLoS Pathog"},{"issue":"6","key":"ppat.1013911.ref005","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1007\/s00109-004-0534-3","article-title":"Prion protein conversion in vitro","volume":"82","author":"S Supattapone","year":"2004","journal-title":"J Mol Med (Berl)"},{"key":"ppat.1013911.ref006","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1007\/128_2011_165","article-title":"Prion protein and its conformational conversion: a structural perspective","author":"WK Surewicz","year":"2011","journal-title":"Prion Proteins"},{"issue":"6936","key":"ppat.1013911.ref007","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1038\/423127a","article-title":"Prion diseases: Cannibals and garbage piles","volume":"423","author":"A Aguzzi","year":"2003","journal-title":"Nature"},{"issue":"5","key":"ppat.1013911.ref008","doi-asserted-by":"crossref","first-page":"1558","DOI":"10.1128\/jvi.62.5.1558-1564.1988","article-title":"Scrapie-infected murine neuroblastoma cells produce protease-resistant prion proteins","volume":"62","author":"DA Butler","year":"1988","journal-title":"J Virol"},{"issue":"33","key":"ppat.1013911.ref009","doi-asserted-by":"crossref","first-page":"12271","DOI":"10.1073\/pnas.0402725101","article-title":"Prions can infect primary cultured neurons and astrocytes and promote neuronal cell death","volume":"101","author":"S Cronier","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"5","key":"ppat.1013911.ref010","doi-asserted-by":"crossref","first-page":"2535","DOI":"10.1128\/JVI.03082-12","article-title":"Prion propagation and toxicity occur in vitro with two-phase kinetics specific to strain and neuronal type","volume":"87","author":"S Hannaoui","year":"2013","journal-title":"J Virol"},{"issue":"8","key":"ppat.1013911.ref011","doi-asserted-by":"crossref","first-page":"2845","DOI":"10.1128\/jvi.62.8.2845-2849.1988","article-title":"Analyses of frequency of infection, specific infectivity, and prion protein biosynthesis in scrapie-infected neuroblastoma cell clones","volume":"62","author":"RE Race","year":"1988","journal-title":"J Virol"},{"issue":"2","key":"ppat.1013911.ref012","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1111\/bpa.12694","article-title":"Prion neurotoxicity","volume":"29","author":"NTT Le","year":"2019","journal-title":"Brain Pathol"},{"issue":"6563","key":"ppat.1013911.ref013","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1038\/379339a0","article-title":"Normal host prion protein necessary for scrapie-induced neurotoxicity","volume":"379","author":"S Brandner","year":"1996","journal-title":"Nature"},{"issue":"5646","key":"ppat.1013911.ref014","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1126\/science.1090187","article-title":"Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis","volume":"302","author":"G Mallucci","year":"2003","journal-title":"Science"},{"issue":"3","key":"ppat.1013911.ref015","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.neuron.2007.01.005","article-title":"Targeting cellular prion protein reverses early cognitive deficits and neurophysiological dysfunction in prion-infected mice","volume":"53","author":"GR Mallucci","year":"2007","journal-title":"Neuron"},{"issue":"5727","key":"ppat.1013911.ref016","doi-asserted-by":"crossref","first-page":"1420","DOI":"10.1126\/science.1114168","article-title":"Cell biology. 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Talan","year":"2010","journal-title":"Neurology Today"},{"issue":"1","key":"ppat.1013911.ref032","doi-asserted-by":"crossref","first-page":"13211","DOI":"10.1038\/s41598-018-31394-6","article-title":"Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease","volume":"8","author":"Z Zheng","year":"2018","journal-title":"Sci Rep"},{"issue":"2","key":"ppat.1013911.ref033","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/j.celrep.2013.06.030","article-title":"Thermodynamic stabilization of the folded domain of prion protein inhibits prion infection in vivo","volume":"4","author":"Q Kong","year":"2013","journal-title":"Cell Rep"},{"issue":"7","key":"ppat.1013911.ref034","article-title":"PRNP allelic series from 19 years of prion protein gene sequencing at the MRC Prion Unit","volume":"31","author":"JA Beck","year":"2010","journal-title":"Hum 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