Prion diseases articles within Nature Communications

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  • Article
    | Open Access

    In this work, the authors investigated the cellular mode of prion propagation. The report that proteopathic seeds of abnormal PrP are N-terminally truncated and detected within minutes after infection. These seeds reach the plasma membrane by regulated secretory pathways where phenotypically distinct fibril-like PrP aggregates are formed with a lag of 24 h after infection.

    • Juan Manuel Ribes
    • , Mitali P. Patel
    •  & Peter-Christian Klöhn

  • Article
    | Open Access

    There are currently no validated methods for the diagnosis of prion disease at the preclinical stage. Here the authors show that serial protein misfolding cyclic amplification and real-time quaking-induced conversion can be used to detect prions in the skin of prion-inoculated hamsters and humanized transgenic mice at early preclinical stages.

    • Zerui Wang
    • , Matteo Manca
    •  & Wen-Quan Zou

  • Article
    | Open Access

    Synthetic prions have previously been generated from recombinant rodent PrP. Here the authors generate synthetic human prions, by seeding human PrP with CJD prions, and characterize its infectivity in mice.

    • Chae Kim
    • , Xiangzhu Xiao
    •  & Jiri G. Safar

  • Article
    | Open Access

    It is hypothesised that exposure to bovine spongiform encephalopathy through contaminated food could have resulted in a large proportion of latent variant Creutzfeldt-Jakob disease cases in humans. Here the authors demonstrate that inoculation with blood from non-symptomatic, vCJD infected humans, results in a unique prion-like disorder in mice and macaques.

    • Emmanuel E. Comoy
    • , Jacqueline Mikol
    •  & Jean-Philippe Deslys

  • Article |

    Scrapie, a form of prion disease that affects sheep and goats, is believed not to be transmissible to humans. Using transgenic mice expressing human prion protein as a model of cross-species prion transmission, the authors show that ovine scrapie may possess potential to be passed on to humans.

    • Hervé Cassard
    • , Juan-Maria Torres
    •  & Olivier Andréoletti

  • Article
    | Open Access

    Prions (PrP) are infectious agents that cause lethal neurodegenerative diseases. Here the authors study the kinetics of prion propagation in mice and show that the onset of neuropathology occurs during the late phase of disease and is hypothesized to be due to increases in a toxic isoform of PrP that is different from the infectious species.

    • Malin K. Sandberg
    • , Huda Al-Doujaily
    •  & John Collinge

  • Article |

    Prion protein accumulation in endosomal vesicles has been implicated in the progression of prion diseases. Uchiyama and colleagues infect neuronal cells with prion proteins and find that this delays post-Golgi vesicular trafficking of membrane proteins and impairs insulin signalling.

    • Keiji Uchiyama
    • , Naomi Muramatsu
    •  & Suehiro Sakaguchi

  • Article
    | Open Access

    Prion proteins are implicated in a range of neurodegenerative diseases, which are, in part, due to a disruption of metal homeostasis. Wattet al.use selective antagonists to show that prion proteins mediate zinc uptake by interacting with GluA2-lacking, GluA1-containing AMPA receptors.

    • Nicole T. Watt
    • , David R. Taylor
    •  & Nigel M. Hooper

  • Article |

    Bioassays are the standard way to measure prion infectivity titres, but can be time-consuming. In this study, bioassays are compared with a modified version of the protein misfolding cyclic amplification technique with beads (PMCAb), demonstrating that PMCAb can be more precise and faster than bioassays.

    • Natallia Makarava
    • , Regina Savtchenko
    •  & Ilia V. Baskakov

  • Article
    | Open Access

    The study of prion diseases has been hampered as there is no method to distinguish newly formed abnormal prion protein conformers. Here, the authors describe a method to study newly formed abnormal prion protein and demonstrate that it is produced within 1 minute of cell exposure to prions.

    • R. Goold
    • , S. Rabbanian
    •  & S.J. Tabrizi

  • Article
    | Open Access

    The infectious prion diseases affect numerous hoofed animal species, and it has been suggested that the properties of the local soil affect transmission of these diseases. Here, the authors studied two North American locations and demonstrate that soil clay content can influence the infection rate in deer.

    • W. David Walter
    • , Daniel P. Walsh
    •  & Michael W. Miller

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