{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T03:06:48Z","timestamp":1789787208930,"version":"4.0.1"},"reference-count":64,"publisher":"The Royal Society","issue":"11","license":[{"start":{"date-parts":[[2017,11,1]],"date-time":"2017-11-01T00:00:00Z","timestamp":1509494400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2017,11,1]],"date-time":"2017-11-01T00:00:00Z","timestamp":1509494400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"US National Institutes of Health","doi-asserted-by":"crossref","award":["AG047505"],"award-info":[{"award-number":["AG047505"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100000265","name":"UK Medical Research Council","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100000265","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["royalsocietypublishing.org"],"crossmark-restriction":true},"short-container-title":["Open Biol."],"published-print":{"date-parts":[[2017,11]]},"abstract":"<jats:p>\n            Mammalian prions cause lethal neurodegenerative diseases such as Creutzfeldt\u2013Jakob disease (CJD) and consist of multi-chain assemblies of misfolded cellular prion protein (PrP\n            <jats:sup>C<\/jats:sup>\n            ). Ligands that bind to PrP\n            <jats:sup>C<\/jats:sup>\n            can inhibit prion propagation and neurotoxicity. Extensive prior work established that certain soluble assemblies of the Alzheimer's disease (AD)-associated amyloid \u03b2-protein (A\u03b2) can tightly bind to PrP\n            <jats:sup>C<\/jats:sup>\n            , and that this interaction may be relevant to their toxicity in AD. Here, we investigated whether such soluble A\u03b2 assemblies might, conversely, have an inhibitory effect on prion propagation. Using cellular models of prion infection and propagation and distinct A\u03b2 preparations, we found that the form of A\u03b2 assemblies which most avidly bound to PrP\n            <jats:italic>in vitro<\/jats:italic>\n            also inhibited prion infection and propagation. By contrast, forms of A\u03b2 which exhibit little or no binding to PrP were unable to attenuate prion propagation. These data suggest that soluble aggregates of A\u03b2 can compete with prions for binding to PrP\n            <jats:sup>C<\/jats:sup>\n            and emphasize the bidirectional nature of the interplay between A\u03b2 and PrP\n            <jats:sup>C<\/jats:sup>\n            in Alzheimer's and prion diseases. Such inhibitory effects of A\u03b2 on prion propagation may contribute to the apparent fall-off in the incidence of sporadic CJD at advanced age where cerebral A\u03b2 deposition is common.\n          <\/jats:p>","DOI":"10.1098\/rsob.170158","type":"journal-article","created":{"date-parts":[[2017,11,15]],"date-time":"2017-11-15T10:10:15Z","timestamp":1510740615000},"update-policy":"https:\/\/doi.org\/10.1098\/crossmark-policy","source":"Crossref","is-referenced-by-count":15,"title":["Soluble A\u03b2 aggregates can inhibit prion propagation"],"prefix":"10.1098","volume":"7","author":[{"given":"Claire J.","family":"Sarell","sequence":"first","affiliation":[{"name":"MRC Prion Unit at UCL, UCL Institute of Prion Diseases, National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emma","family":"Quarterman","sequence":"additional","affiliation":[{"name":"MRC Prion Unit at UCL, UCL Institute of Prion Diseases, National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel C.-M.","family":"Yip","sequence":"additional","affiliation":[{"name":"MRC Prion Unit at UCL, UCL Institute of Prion Diseases, National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cassandra","family":"Terry","sequence":"additional","affiliation":[{"name":"MRC Prion Unit at UCL, UCL Institute of Prion Diseases, National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew J.","family":"Nicoll","sequence":"additional","affiliation":[{"name":"MRC Prion Unit at UCL, UCL Institute of Prion Diseases, National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4797-2259","authenticated-orcid":false,"given":"Jonathan D. F.","family":"Wadsworth","sequence":"additional","affiliation":[{"name":"MRC Prion Unit at UCL, UCL Institute of Prion Diseases, National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark A.","family":"Farrow","sequence":"additional","affiliation":[{"name":"MRC Prion Unit at UCL, UCL Institute of Prion Diseases, National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0718-6261","authenticated-orcid":false,"given":"Dominic M.","family":"Walsh","sequence":"additional","affiliation":[{"name":"MRC Prion Unit at UCL, UCL Institute of Prion Diseases, National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK"},{"name":"Laboratory for Neurodegenerative Research, Ann Romney Center for Neurologic Diseases, Brigham and Women's Hospital, Harvard Medical 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