A View from the Top--Prion Diseases from 10,000 Feet

  title={A View from the Top--Prion Diseases from 10,000 Feet},
  author={Suzette A. Priola and Bruce W. Chesebro and Byron Caughey},
  pages={917 - 919}
The transmissible spongiform encephalopathies or prion diseases include scrapie in sheep, mad cow disease, and variant Creutzfeld-Jakob disease in humans. The agent of all of these diseases is thought to be a self-replicating protein or prion. In a report of a recent meeting on prion diseases, Priola, Chesebro, and Caughey discuss the latest developments in this often contentious field of research. 
Spiroplasma as a Candidate Agent for the Transmissible Spongiform Encephalopathies
  • F. Bastian
  • Biology, Medicine
  • Journal of neuropathology and experimental neurology
  • 2005
Data from an epidemiologic infection model evidence accumulated over the past 30 years showing involvement of Spiroplasma infection in TSE support the hypothesis that a SpiroPLasma sp. Expand
Insights into prion strains and neurotoxicity
Prion strains are TSE isolates that, after inoculation into distinct hosts, cause disease with consistent characteristics, such as incubation period, distinct patterns of PrPSc distribution and spongiosis and relative severity of the spongiform changes in the brain. Expand
Slow virus disease: Deciphering conflicting data on the transmissible spongiform encephalopathies (TSE) also called prion diseases
Current pathogen‐cell plasma membrane properties are reviewed, showing that the primary biochemical marker of the prion disease is used as a receptor by the intracellular bacterium Brucella abortus, and supports the concept that Spiroplasma, a wall‐less bacterium, may be a transmissible agent of TSE. Expand
Prion - A Review
The different modes of transmission of different prion diseases, the unpredictable species barriers, the variable distribution of infectivity in tissues, and strain variations found in some diseases all make risk assessment and predictions of future events difficult. Expand
Progress and problems in the biology, diagnostics, and therapeutics of prion diseases.
Recent progress in the areas of pathogenesis of, diagnostics of, and therapy for prion diseases is reviewed and some conspicuous problems that remain to be addressed are highlighted. Expand
1 Endogenous Viral Etiology of Prion Diseases
Transmissible spongiform encephalopathies (TSEs), or prion diseases, are a group of incurable neurodegenerative disorders, including Kuru and Creutzfeldt-Jakob disease in humans, “mad cow” disease inExpand
Endogenous Viral Etiology of Prion Diseases
The endogenous TSE virus model is consistent with the TSE data and offers solutions to many enigmatic features associated with TSE, including the function of PrP that, despite more than two decades of TSE research conducted within the framework of the prion hypothesis, is still not known. Expand
Chirality of the Disulfide in the Prion Proteins
  • M. Carmack
  • Chemistry, Medicine
  • J. Chem. Inf. Model.
  • 2004
It is suggested that handedness in the disulfide bond of prions may transmit stereochemical information that can influence the manner of folding or refolding into pathogenic forms. Expand
Prions and peripheral nerves: A deadly rendezvous
The mechanisms of neuronal prion transport from the periphery into the CNS or vice versa are heavily investigated and debated but poorly understood. Expand
Acute cellular uptake of abnormal prion protein is cell type and scrapie-strain independent.
PrP-res uptake was rapid and independent of scrapie strain, cell type, or cellular PrP expression, but occurred in only a subset of cells and was influenced by PrP- Res preparation and aggregate size, which can all influence whether or not a cell takes up Prp-res following exposure to TSE infectivity. Expand


Soluble Dimeric Prion Protein Binds PrPSc In Vivo and Antagonizes Prion Disease
In wild-type mice, the expression of PrP(C) rendered soluble and dimeric by fusion to immunoglobulin Fcgamma (PrP-Fc(2) delays prP(Sc) accumulation, agent replication, and onset of disease following inoculation with infective prions. Expand