Annals of Indian Academy of Neurology
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REVIEW ARTICLE
Year : 2016  |  Volume : 19  |  Issue : 2  |  Page : 169-174

Prions, prion-like prionoids, and neurodegenerative disordersVacancy


Department of Neurology, Miller School of Medicine, University of Miami, Miami, Florida, USA

Correspondence Address:
Ashok Verma
Clinical Research Building, 1120 NW 14 Street, Suite 1317, Miami, Florida - 33136
USA
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Source of Support: None, Conflict of Interest: None


DOI: 10.4103/0972-2327.179979

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Prion diseases or transmissible spongiform encephalopathies are fatal neurodegenerative diseases characterized by the aggregation and deposition of the misfolded prion protein in the brain. α-synuclein (α-syn)-associated multiple system atrophy has been recently shown to be caused by a bona fide α-syn prion strain. Several other misfolded native proteins such as β-amyloid, tau and TDP-43 share some aspects of prions although none of them is shown to be transmissible in nature or in experimental animals. However, these prion-like “prionoids” are causal to a variety of neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis. The remarkable recent discovery of at least two new α-syn prion strains and their transmissibility in transgenic mice and in vitro cell models raises a distinct question as to whether some specific strain of other prionoids could have the capability of disease transmission in a manner similar to prions. In this overview, we briefly describe human and other mammalian prion diseases and comment on certain similarities between prion and prionoid and the possibility of prion-like transmissibility of some prionoid strains.


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