PrPSc prions : : state of the art / / edited by Joaquín Castilla, Jesús R. Requena.

• TeilnehmendeR: Castilla, Joaquín,; Requena, Jesús R.,
• Place / Publishing House: Basel, Switzerland : : MDPI,, [2018]; ©2018
• Year of Publication: 2018
• Language: English
• Physical Description: 1 online resource (210 pages) :; illustrations

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.

Table of Contents

About the Special Issue Editors . vii -- Preface to "PrPSc Prions: State of the Art" . ix -- Daniel Hughes and Mark Halliday What Is Our Current Understanding of PrPSc-Associated Neurotoxicity and Its Molecular Underpinnings? Reprinted from: Pathogens 2017, 6, 63, doi: 10.3390/pathogens6040063 . 1 -- Maria Letizia Barreca, Nunzio Iraci, Silvia Biggi, Violetta Cecchetti and Emiliano Biasini Pharmacological Agents Targeting the Cellular Prion Protein Reprinted from: Pathogens 2018, 7, 27, doi: 10.3390/pathogens7010027 . 23 -- Jos ´e Miguel Flores-Fern´andez, Vineet Rathod and Holger Wille Comparing the Folds of Prions and Other Pathogenic Amyloids Reprinted from: Pathogens 2018, 7, 50, doi: 10.3390/pathogens7020050 . 39 -- Nicholas J. Haley and J ¨urgen A. Richt Evolution of Diagnostic Tests for Chronic Wasting Disease, a Naturally Occurring Prion Disease of Cervids Reprinted from: Pathogens 2017, 6, 35, doi: 10.3390/pathogens6030035 . 53 -- Holger Wille and Jes ´us R. Requena The Structure of PrPSc Prions Reprinted from: Pathogens 2018, 7, 20, doi: 10.3390/pathogens7010020 . 75 -- Jian Hu, Holger Wille and Gerold Schmitt-Ulms The Evolutionary unZIPping of a Dimerization Motif-A Comparison of ZIP and PrP Architectures Reprinted from: Pathogens 2018, 7, 4, doi: 10.3390/pathogens7010004 86 -- Jorge M. Charco, Hasier Erana, ˜ Vanessa Venegas, Sandra Garc´ıa-Mart´ınez, Rafael Lopez-Moreno, ´ Ezequiel Gonz´alez-Miranda, Miguel Angel ´ P´erez-Castro and Joaqu´ın Castilla Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies Reprinted from: Pathogens 2017, 6, 67, doi: 10.3390/pathogens6040067 . 97 -- Neil A. Mabbott How do PrPSc Prions Spread between Host Species, and within Hosts? Reprinted from: Pathogens 2017, 6, 60, doi: 10.3390/pathogens6040060 . 117 -- Amber Roguski and Andrew C. Gill The Role of the Mammalian Prion Protein in the Control of Sleep Reprinted from: Pathogens 2017, 6, 58, doi: 10.3390/pathogens6040058 . 158 -- Ang ´elique Igel-Egalon, Vincent B´eringue, Human Rezaei and Pierre Sibille Prion Strains and Transmission Barrier Phenomena Reprinted from: Pathogens 2018, 7, 5, doi: 10.3390/pathogens7010005 170.