Definition and research guide
This page combines a MeSH definition, publication statistics and selected research abstracts. It is a starting point for reading the literature, not a medical textbook or a systematic evidence review.
Content available: 4 complete abstracts (730 words), 10 references. Full article text is not stored or reproduced here; follow the PMID, DOI or PMC links to read the original sources and their access terms.
Definition
A fatal disease of the nervous system in sheep and goats, characterized by pruritus, debility, and locomotor incoordination. It is caused by proteinaceous infectious particles called prions.
Definition: NLM Medical Subject Headings (MeSH) scope note (Public domain (U.S. National Library of Medicine); attribution requested). View the MeSH record.
Also known as: Rida.
Where it fits in the MeSH classification
- Broader topics
- Prion Diseases; Sheep Diseases
- See also
- Prions; Prion Diseases; PrPSc Proteins
Related concepts
- Prions
Research landscape
PubMed indexes 3,463 records tagged with the MeSH heading “Scrapie” (counts retrieved 2026-10-29). 170 of them (4.9%) were published from 2020 onward, and the busiest period so far is through 1999 with 1,525 records.
Reviews account for 414 records (12.0%) and meta-analyses for 2. Randomized controlled trials number 1 (0.0%) as a share of all records on the topic. Randomized trials make up only a small share of this literature, so much of what is known comes from laboratory, observational or descriptive work.
Show the data
| Period | Records |
|---|---|
| through 1999 | 1,525 |
| 2000-2009 | 1,174 |
| 2010-2019 | 594 |
| 2020 onward | 170 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 414 | 12.0% |
| Meta-analyses | 2 | 0.1% |
| Randomized controlled trials | 1 | 0.0% |
Method: PubMed query "Scrapie"[MeSH Terms] with publication-type and date filters, retrieved 2026-10-29.
Reading the evidence in infectious diseases
Infectious disease evidence combines microbiology, epidemiology and clinical trials. Laboratory studies identify pathogens and how they cause harm; surveillance and outbreak investigations describe who is affected and how infection spreads; trials establish whether treatments and vaccines work. Results depend on place and time, because pathogens evolve and resistance patterns and population immunity change. Check when and where the data were collected, how cases were defined and how up to date the evidence is.
Evidence from open-access studies
These open-access studies come from PubMed’s best-match results for this heading (papers whose main topic it is), ranked here by citation count, with one recent addition. Each abstract is reproduced in full under its recorded open licence so that you can read the authors’ own words. They illustrate the literature; they are not a systematic summary of it. Citation counts measure attention, not reliability or clinical benefit.
| Study / authors | Year | Source label / design | Europe PMC citations | Licence / source |
|---|---|---|---|---|
| A miRNA signature of prion induced neurodegeneration | 2008 | Research article Design not recorded in structured metadata | 196 | cc by PMID 18987751 · DOI · PMC2575400 |
| Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoring | 2010 | Research article Design not recorded in structured metadata | 114 | cc0 PMID 20221436 · DOI · PMC2832701 |
| Cryo-EM structure of anchorless RML prion reveals variations in shared motifs between distinct strains | 2022 | Research article Design not recorded in structured metadata | 84 | cc by PMID 35831291 · DOI · PMC9279418 |
| Evidence for multiple prion conformers in natural scrapie isolates | 2026 | Research article Design not recorded in structured metadata | 0 | cc by PMID 42752506 · DOI · PMC13596833 |
A miRNA signature of prion induced neurodegeneration [1]
Abstract reading summary — source excerpts
- Opening excerpt
- MicroRNAs (miRNAs) are small, non-coding RNA molecules which are emerging as key regulators of numerous cellular processes.
- Closing excerpt
- In particular, a correlation between miRNA expression and putative gene targets involved in intracellular protein-degradation pathways and signaling pathways related to cell death, synapse function and neurogenesis was identified.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (204 words)
MicroRNAs (miRNAs) are small, non-coding RNA molecules which are emerging as key regulators of numerous cellular processes. Compelling evidence links miRNAs to the control of neuronal development and differentiation, however, little is known about their role in neurodegeneration. We used microarrays and RT-PCR to profile miRNA expression changes in the brains of mice infected with mouse-adapted scrapie. We determined 15 miRNAs were de-regulated during the disease processes; miR-342-3p, miR-320, let-7b, miR-328, miR-128, miR-139-5p and miR-146a were over 2.5 fold up-regulated and miR-338-3p and miR-337-3p over 2.5 fold down-regulated. Only one of these miRNAs, miR-128, has previously been shown to be de-regulated in neurodegenerative disease. De-regulation of a unique subset of miRNAs suggests a conserved, disease-specific pattern of differentially expressed miRNAs is associated with prion-induced neurodegeneration. Computational analysis predicted numerous potential gene targets of these miRNAs, including 119 genes previously determined to be also de-regulated in mouse scrapie. We used a co-ordinated approach to integrate miRNA and mRNA profiling, bioinformatic predictions and biochemical validation to determine miRNA regulated processes and genes potentially involved in disease progression. In particular, a correlation between miRNA expression and putative gene targets involved in intracellular protein-degradation pathways and signaling pathways related to cell death, synapse function and neurogenesis was identified.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 18987751 · DOI · PMC2575400
Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoring [2]
Abstract reading summary — source excerpts
- Opening excerpt
- Prion diseases are fatal neurodegenerative diseases of humans and animals characterized by gray matter spongiosis and accumulation of aggregated, misfolded, protease-resistant prion protein (PrPres).
- Closing excerpt
- These findings were similar to certain human familial prion diseases as well as to non-prion human neurodegenerative diseases, such as Alzheimer's disease.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (221 words)
Prion diseases are fatal neurodegenerative diseases of humans and animals characterized by gray matter spongiosis and accumulation of aggregated, misfolded, protease-resistant prion protein (PrPres). PrPres can be deposited in brain in an amyloid-form and/or non-amyloid form, and is derived from host-encoded protease-sensitive PrP (PrPsen), a protein normally anchored to the plasma membrane by glycosylphosphatidylinositol (GPI). Previously, using heterozygous transgenic mice expressing only anchorless PrP, we found that PrP anchoring to the cell membrane was required for typical clinical scrapie. However, in the present experiments, using homozygous transgenic mice expressing two-fold more anchorless PrP, scrapie infection induced a new fatal disease with unique clinical signs and altered neuropathology, compared to non-transgenic mice expressing only anchored PrP. Brain tissue of transgenic mice had high amounts of infectivity, and histopathology showed dense amyloid PrPres plaque deposits without gray matter spongiosis. In contrast, infected non-transgenic mice had diffuse non-amyloid PrPres deposits with significant gray matter spongiosis. Brain graft studies suggested that anchored PrPsen expression was required for gray matter spongiosis during prion infection. Furthermore, electron and light microscopic studies in infected transgenic mice demonstrated several pathogenic processes not seen in typical prion disease, including cerebral amyloid angiopathy and ultrastructural alterations in perivascular neuropil. These findings were similar to certain human familial prion diseases as well as to non-prion human neurodegenerative diseases, such as Alzheimer's disease.
Abstract reproduced from the open-access article under the recorded cc0 licence; © the authors. PMID 20221436 · DOI · PMC2832701
Cryo-EM structure of anchorless RML prion reveals variations in shared motifs between distinct strains [3]
Abstract reading summary — source excerpts
- Opening excerpt
- Little is known about the structural basis of prion strains.
- Closing excerpt
- This work demonstrates both common and divergent structural features of prion strains at the near-atomic level.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (147 words)
Little is known about the structural basis of prion strains. Here we provide a high (3.0 Å) resolution cryo-electron microscopy-based structure of infectious brain-derived fibrils of the mouse anchorless RML scrapie strain which, like the recently determined hamster 263K strain, has a parallel in-register β-sheet-based core. Several structural motifs are shared between these ex vivo prion strains, including an amino-proximal steric zipper and three β-arches. However, detailed comparisons reveal variations in these shared structural topologies and other features. Unlike 263K and wildtype RML prions, the anchorless RML prions lack glycophosphatidylinositol anchors and are severely deficient in N-linked glycans. Nonetheless, the similarity of our anchorless RML structure to one reported for wildtype RML prion fibrils in an accompanying paper indicates that these post-translational modifications do not substantially alter the amyloid core conformation. This work demonstrates both common and divergent structural features of prion strains at the near-atomic level.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 35831291 · DOI · PMC9279418
Evidence for multiple prion conformers in natural scrapie isolates [4]
Abstract reading summary — source excerpts
- Opening excerpt
- Prion strains in infected animals may exist as heterogeneous populations composed of a major prion conformer responsible for the dominant disease phenotype and minor conformers that are phenotypically silent or difficult to detect.
- Closing excerpt
- These findings support the idea that scrapie prion populations can contain diverse conformers and that changes in detectable conformer populations during passage may contribute to the overall diversity of scrapie prions.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (158 words)
Prion strains in infected animals may exist as heterogeneous populations composed of a major prion conformer responsible for the dominant disease phenotype and minor conformers that are phenotypically silent or difficult to detect. However, the presence and biological significance of such minor conformers in natural prion isolates remain poorly understood. Identifying and characterizing these hidden substrains is important for understanding prion strain diversity and for assessing potential transmission risks to humans and livestock. In this study, we utilized a modified protein misfolding cyclic amplification (PMCA) method to detect substrains within classical scrapie isolates. Our analysis provided evidence consistent with the coexistence of multiple prion conformers, including previously unrecognized conformers, within single prion isolates. Furthermore, we observed changes in the detectable substrain composition during passages in animal hosts. These findings support the idea that scrapie prion populations can contain diverse conformers and that changes in detectable conformer populations during passage may contribute to the overall diversity of scrapie prions.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 42752506 · DOI · PMC13596833
Key reviews and meta-analyses
The most cited review-type papers among PubMed’s best-match results for this heading, listed with bibliographic details only. Follow the links for the full text and access terms.
- Research article Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? [5]
- Research article Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins [6]
- Research article Transmission of bovine spongiform encephalopathy and scrapie to mice: strain variation and the species barrier [7]
- Research article Scrapie strain variation and mutation [8]
- Research article Atypical/Nor98 scrapie: properties of the agent, genetics, and epidemiology [9]
- Research article The genetics of scrapie in sheep and goats [10]
References
- Saba R, Goodman CD, Huzarewich RL, Robertson C, Booth SA. A miRNA signature of prion induced neurodegeneration. . 2008. PMID 18987751 · DOI · PMC2575400
- Chesebro B, Race B, Meade-White K, Lacasse R, Race R, Klingeborn M, et al.. Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoring. . 2010. PMID 20221436 · DOI · PMC2832701
- Hoyt F, Standke HG, Artikis E, Schwartz CL, Hansen B, Li K, et al.. Cryo-EM structure of anchorless RML prion reveals variations in shared motifs between distinct strains. . 2022. PMID 35831291 · DOI · PMC9279418
- Imamura M, Miyazawa K, Okada H, Ohno M, Iguchi H, Matsuura Y, et al.. Evidence for multiple prion conformers in natural scrapie isolates. . 2026. PMID 42752506 · DOI · PMC13596833
- Jarrett JT, Lansbury PT. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?. Cell. 1993. PMID 8513491 · DOI
- Harper JD, Lansbury PT. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem. 1997. PMID 9242912 · DOI
- Bruce M, Chree A, McConnell I, Foster J, Pearson G, Fraser H. Transmission of bovine spongiform encephalopathy and scrapie to mice: strain variation and the species barrier. Philos Trans R Soc Lond B Biol Sci. 1994. PMID 7913758 · DOI
- Bruce ME. Scrapie strain variation and mutation. Br Med Bull. 1993. PMID 8137131 · DOI
- Benestad SL, Arsac JN, Goldmann W, Nöremark M. Atypical/Nor98 scrapie: properties of the agent, genetics, and epidemiology. Vet Res. 2008. PMID 18187032 · DOI
- Baylis M, Goldmann W. The genetics of scrapie in sheep and goats. Curr Mol Med. 2004. PMID 15354869 · DOI
About this article
- Sources
- NLM Medical Subject Headings (definition, synonyms); NCBI PubMed (counts, identifiers); Europe PMC (open-access abstracts and citation counts).
- Verification
- Every reference was resolved against PubMed on 2026-10-31; title, year and DOI matched.
- Review state
- automated source verified; no human expert review has been recorded yet.
- Version
- 1, last updated 2026-10-29.
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Evidence strength
EvidenceHelix's computed view of the study designs behind this topic: how common meta-analyses, randomized trials and reviews are, how recent the literature is, and a plain-language reading. It describes the design mix of the literature. It is not a quality appraisal of any study, and it is not medical advice.