Journal article Open Access

Prion-like disorders and Transmissible Spongiform Encephalopathies: An overview of the mechanistic features that are shared by the various disease-related misfolded proteins

Eraña, Hasier; Venegas, Vanesa; Moreno, Jorge; Castilla, Joaquín

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    <subfield code="a">Prion diseases or Transmissible Spongiform Encephalopathies
(TSEs) are a group of fatal neurodegenerative disorders affecting several
mammalian species. Its causative agent, disease-associated prion protein
(PrPd), is a self-propagating β-sheet rich aberrant conformation of the
cellular prion protein (PrPC) with neurotoxic and aggregation-prone
properties, capable of inducing misfolding of PrPC molecules. PrPd is the
major constituent of prions and, most importantly, is the first known
example of a protein with infectious attributes. It has been suggested
that similar molecular mechanisms could be shared by other proteins
implicated in diseases such as Alzheimer's disease, Parkinson's disease,
amyotrophic lateral sclerosis or systemic amyloidoses. Accordingly,
several terms have been proposed to collectively group all these
disorders. Through the stringent evaluation of those aspects that
characterise TSE-causing prions, in particular propagation and spread,
strain variability or transmissibility, we will discuss whether terms
such as "prion", "prion-like", "prionoid" or "propagon" can be used when
referring to the aetiological agents of the above other disorders.
Moreover, it will also be discussed whether the term "infectious", which
defines a prion essential trait, is currently misused when referring to
the other misfolded proteins.</subfield>
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