Reprint

PrPSc Prions: State of the Art

Edited by
October 2018
210 pages
  • ISBN978-3-03897-308-9 (Paperback)
  • ISBN978-3-03897-309-6 (PDF)

This book is a reprint of the Special Issue PrPSc prions: state of the art that was published in

Biology & Life Sciences
Medicine & Pharmacology
Public Health & Healthcare
Summary
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a group of fatal and transmissible neurodegenerative disorders characterized by long incubation periods, misfolded prion protein (PrP) deposition, and usually spongiform vacuolation. These devastating diseases affect many mammals, with the best known examples being Creutzfeldt–Jakob disease (CJD), fatal familial insomnia (FFI), or Kuru in humans; and scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle, and chronic wasting disease (CWD) in cervids. Despite major achievements in research of TSEs, there are still many unresolved key issues that hamper the development of effective therapies. However, the last decade has been particularly prolific in advances in the prion field. Among others, prion propagation in vitro has been achieved, leading to new diagnostic methods; the basic architecture of infectious prions has been deciphered; new prion disease types have been described in humans and other animals; and prion disorders have emerged in places that had not previously reported the disorders, as is the case for CWD in Europe.This Special Issue will focus on the state of the art of our knowledge of PrPSc: on what we know about its structure and propagation, the basis of strains and transmission barriers, the mechanisms of PrPSc toxicity, the possible function of PrPSc’s properly folded precursor, PrPC and its evolutionary history, and recent technical breakthroughs in diagnostics and therapy development among other key aspects of PrPSc prion biology.
Format
  • Paperback
License
© 2018 by the authors; CC BY-NC-ND license
Keywords
prion; cervids; PMCA; RT-QuIC; diagnosis; prion; sleep; circadian rhythm; melatonin; serotonin; prions; prion protein; PrPSc; horizontal transmission; vertical transmission; secondary lymphoid organs; intestine; central nervous system; prion disease; neurodegeneration; neurotoxicity; proteostasis; PrPSc; Prion disease; TSE; recombinant PrP; in vitro propagation; PMCA; QuIC; ZIP metal ion transporter; prion protein; dimerization; evolution; prion strain; species barrier; strain adaptation; zoonosis; Darwinian evolution; deformed templating; structural elementary brick; PrPSc; prion structure; β-solenoid; cryo-electron microscopy; prion propagation; amyloid; cellular prion protein; prion diseases; PrP ligands; pharmacological chaperones; prion structure; β-solenoid; PHF-tau structure; Aβ(1-42) fibril structure; α-synuclein amyloid structure; parallel in-register β-structure