Journal
JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY
Volume 70, Issue 5, Pages 377-385Publisher
OXFORD UNIV PRESS INC
DOI: 10.1097/NEN.0b013e318217d95f
Keywords
alpha-Synuclein; Bovine spongiform encephalopathy; Prion; Scrapie
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Funding
- ANRT, Paris, France (Association Nationale pour la Recherche et la Technologie) [CIFRE 2006/1050]
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There is a growing interest in the potential roles of misfolded protein interactions in neurodegeneration. To investigate this issue, we inoculated 3 prion strains intracerebrally into transgenic (TgM83) mice that overexpress human A53T alpha-synuclein. In comparison to nontransgenic controls, there was a striking decrease in the incubation periods of scrapie, classic and H-type bovine spongiform encephalopathies (C-BSE and H-BSE), with conservation of the histopathologic and biochemical features characterizing these 3 prion strains. TgM83 mice died of scrapie or C-BSE prion diseases before accumulating the insoluble and phosphorylated forms of alpha-synuclein specific to late stages of synucleinopathy. In contrast, the median incubation time for TgM83 mice inoculated with H-BSE was comparable to that observed when these mice were uninfected, thereby allowing the development of molecular alterations of alpha-synuclein. The last 4 mice of this cohort exhibited early accumulations of H-BSE prion protein along with alpha-synuclein pathology. The results indicate that a prion disease was triggered concomitantly with an overt synucleinopathy in some transgenic mice overexpressing human A53T alpha-synuclein after intracerebral inoculation with an H-BSE prion strain.
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