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Squirrel monkeys infected with the classical bovine spongiform encephalopathy agent developed an encephalopathy resembling variant Creutzfeldt\u2013Jakob disease with accumulations not only of abnormal prion protein (PrP<jats:sup>TSE<\/jats:sup>), but also three other proteins: hyperphosphorylated tau (p-tau), \u03b1-synuclein and ubiquitin; \u03b2-amyloid protein (A\u03b2) did not accumulate. Severity of brain lesions correlated with spongiform degeneration. No amyloid was detected. These results suggested that PrP<jats:sup>TSE<\/jats:sup>enhanced formation of p-tau and aggregation of \u03b1-synuclein and ubiquitin, but not A\u03b2, providing a new experimental model for neurodegenerative diseases associated with complex proteinopathies.<\/jats:p>","DOI":"10.1099\/vir.0.062083-0","type":"journal-article","created":{"date-parts":[[2014,4,26]],"date-time":"2014-04-26T05:19:41Z","timestamp":1398489581000},"page":"1612-1618","source":"Crossref","is-referenced-by-count":8,"title":["Complex proteinopathy with accumulations of prion protein, hyperphosphorylated tau, \u03b1-synuclein and ubiquitin in experimental bovine spongiform encephalopathy of monkeys"],"prefix":"10.1099","volume":"95","author":[{"given":"Pedro","family":"Piccardo","sequence":"first","affiliation":[{"name":"Laboratory of Bacterial and TSE Agents, Division of Emerging Transfusion Transmitted Diseases, Office of Blood Research and Review, Center for Biologics Evaluation and Research, Food and Drug 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