Special Issue "PrPSc prions: state of the art"
A special issue of Pathogens (ISSN 2076-0817).
Deadline for manuscript submissions: closed (15 September 2017).
A printed edition of this Special Issue is available here.
2. IKERBASQUE, Basque Foundation for Science, Bilbao 48011, Bizkaia, Spain
Interests: the molecular mechanisms involved in the prion transmission between different species
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, scrapie in sheep, Bovine spongiform encephalopathy (BSE) in cattle and Chronic wasting disease (CWD) in cervids. The nature of the causal agent has been highly controversial, although it is amply demonstrated and widely accepted now that it is an aberrantly folded prion protein (PrPSc), which transforms the normal cellular prion protein (PrPC) into an infectious and transmissible isoform. Prion diseases can be classified into three different types according to their origin, sporadic (putatively spontaneous), acquired or hereditary. Sporadic prion diseases are the result of an apparently spontaneous misfolding of PrPC in an individual and include sporadic Creutzfeldt-Jakob disease (sCJD), which represents 85–90% of all human prion diseases. There are other infrequent and recently discovered atypical forms of sporadic prion diseases like atypical scrapie in sheep and goats, sporadic Fatal Insomnia (sFI) and variable protease-sensitive prionopathy (VPSPr) in humans. The hereditary or familial forms are associated with a range of dominantly inherited mutations within the open reading frame (ORF) of the prion protein gene (PRNP). More than 30 different pathogenic mutations, which give rise to specific clinically manifested heritable phenotypes, have been described to date and include: genetic CJD (gCJD), Gerstmann-Sträussler-Scheinker syndrome (GSS) and FFI. Finally, the infectious or acquired forms of the disease are due to accidental exposure to prion contaminated tissues and the best-known examples are variant CJD (vCJD) that affects humans that consumed BSE-contaminated products and iatrogenic CJD (iCJD) that arose in the recent past from prion contaminated surgical instruments or tissues from affected donors. Although the measures implemented after the mad-cow disease crisis have practically eliminate the risk of acquired prion diseases, there is no way to reduce sporadic cases, as they develop in an unpredictable way.
Despite major steps forward achieved in the last three decades of research on TSEs, there are still many unresolved key issues that hamper the development of effective therapies. The main remaining questions include the resolution of the three dimensional structure of infectious prions at the atomic level; clarifying the physiological role(s) of native PrPC, understanding the molecular mechanisms ruling the strain variability and interspecies transmission of TSEs, as well as the exact pathogenic mechanism in the course of a prion disorder. However, the last decade has been particularly prolific in advances in the prion field, so that shedding a definitive light on these issues now appears more feasible than ever. Among others, prion propagation in vitro has been achieved, leading to new diagnostic methods and also to the generation of infectious prions using bacterially expressed proteins; the basic architecture of infectious prions has been deciphered; new prion disease types have been described in humans and other animals and well known prion disorders have emerged in continents previously free of them, as it is the case of CWD in Europe. Yet, there is no therapy or treatment available for these fatal disorders, which is the ultimate goal for researchers working on this unusual pathogen.
In this exciting context, Pathogens will launch a Special Issue devoted to “PrPSc Prions: Towards the Final Frontier”. Although the title might seem redundant (“PrPSc prions”), it is now clear that “PrPSc” and “prion” are not synonyms. On the one hand, there are other prions, infectious proteins, in yeasts and fungi. Additionally, there are a number of proteins involved in human pathology that are strong candidates to being granted the status of prions. In particular, Aβ, tau, synuclein, although a very intense controversy exists and the issue is not still settled. This Special Issue will keep away from these other prions and potential prions and focus on PrPSc.
Both original research and review articles are welcomed. Potential topics include, but are not limited to:
- Transmission barriers in prion diseases.
- Pathogenic mechanisms in prion diseases.
- Potential functions of PrPC.
- Towards a definitive diagnosis in prion diseases.
Dr. Joaquín Castilla
Dr. Jesús R. Requena
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- Prion diseases
- Prion propagation
- Prion structure
- Bovine spongiform encephalopathy
- Chronic wasting disease
- Creutzfeldt-Jakob disease
- Gerstmann-Sträussler-Scheinker disease
- Variably protease-sensitive prionopathy