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U.S. Department of Health and Human Services

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J Gen Virol 2014 Jul;95(Pt 7):1612-8

Complex proteinopathy with accumulations of prion protein, hyperphosphorylated tau,alpha-synuclein and ubiquitin in experimental BSE of monkeys.

Piccardo P, Cervenak J, Bu M, Miller L, Asher DM


Proteins aggregate in several slowly progressive neurodegenerative diseases called "proteinopathies." Studies with cell cultures and transgenic mice overexpressing mutated proteins suggested that aggregates of one protein induced misfolding and aggregation of other proteins as well-a possible common mechanism for some neurodegenerative diseases. But most proteinopathies are "sporadic," without gene mutation or overexpression. Thus, proteinopathies in wild-type animals genetically close to humans might be informative. Squirrel monkeys infected with classical bovine spongiform encephalopathy agent developed an encephalopathy resembling variant Creutzfeldt-Jakob disease with accumulations not only of abnormal prion protein (PrPTSE) but also three other proteins: hyperphosphorylated tau (p-tau), alpha-synuclein and ubiquitin; beta amyloid protein (Abeta) did not accumulate. Severity of brain lesions correlated with spongiform degeneration. No amyloid was detected. These results suggest that PrPTSE enhanced formation of p-tau and aggregation of alpha-synuclein and ubiquitin but not Abeta, providing a new experimental model for neurodegenerative diseases associated with complex proteinopathies.

Category: Journal Article
PubMed ID: #24769839 DOI: 10.1099/vir.0.062083-0
Includes FDA Authors from Scientific Area(s): Biologics
Entry Created: 2014-04-29 Entry Last Modified: 2014-09-28