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Prion disease
Other names: Transmissible spongiform encephalopathy (TSE); slow unconventional virus disease[1]
Micrograph showing spongiform degeneration (vacuoles that appear as holes in tissue sections) in the cerebral cortex of Creutzfeldt–Jakob disease. H&E stain, scale bar = 30 microns (0.03 mm).
SpecialtyNeurology
SymptomsDifficulty thinking, personality changes, problems with coordination.[2]
ComplicationsWorsens over time[2]
TypesHuman: Creutzfeldt-Jakob disease (CJD), variant Creutzfeldt-Jakob disease (vCJD), kuru, variably protease-sensitive prionopathy, Gerstmann-Sträussler-Scheinker syndrome, sporadic fatal insomnia[3][2]
Other animals: Bovine spongiform encephalopathy, scrapie, chronic wasting disease, feline spongiform encephalopathy, transmissible mink encephalopathy[2]
CausesPrion[2]
Diagnostic methodSuspected based on examination, confirmed by brain biopsy[2]
TreatmentSupportive care[2]
PrognosisDeath within months to years[3]
FrequencyRare[3]

Prion disease, also known as transmissible spongiform encephalopathy (TSE), is a group of brain diseases that result in the ongoing loss of neurons.[2][4] Symptoms often include difficulty thinking, personality changes, and problems with coordination, which worsens over time.[2] Other symptoms may include jerking movements, trouble sleeping, and seizures.[2] It can take many years from exposure to symptoms onset.[5] However, once symptoms begin death typically occurs within months to years.[3]

The underlying cause is a normally present, but misfolded protein, known as a prion, that results in the misfolding of normal proteins.[2][3] The disease may start spontaneously, result from genetic mutations inherited from a person's parents, or spread between individuals.[2] They may spread by contact with infected tissue or contaminated medical instruments; but, do not spread by air or most forms of casual contact.[2] Diagnosis may be suspected based on examination and confirmed by brain biopsy.[2] They results in tiny holes in the brain giving it a spongy appearance under a microscope.[2]

Diseases in humans include Creutzfeldt-Jakob disease (CJD), variant Creutzfeldt-Jakob disease (vCJD), kuru, variably protease-sensitive prionopathy, Gerstmann-Sträussler-Scheinker syndrome, and sporadic fatal insomnia.[3][2] Diseases in other animals include bovine spongiform encephalopathy (BSE), scrapie, and chronic wasting disease.[2] vCJD is believed to occur from exposure to eating meat from BSE infected cow.[5]

There is no specific treatment or vaccine.[3] Management is supportive care.[2] Normal sterilization does not render prions non-infectious, with instead concentrated bleach in the form of sodium hypochlorite or heating to a minimum of 134 °C is required.[6] Prion diseases are rare.[3] Kuru was the first confirmed disease of this type, being described in 1957.[1]

Signs and symptoms

Symptoms vary, but commonly include personality changes, psychiatric problems such as depression, lack of coordination, and an unsteady gait. People also may experience involuntary jerking movements (myoclonus), unusual sensations, insomnia, confusion, or memory problems. In the later stages of the disease, they have severe mental impairment (dementia) and lose the ability to move or speak.[2]

Cause

Genetics

Familial forms of prion disease are caused by inherited mutations in the PRNP gene. Only a small percentage of all cases of prion disease run in families, however. Most cases of prion disease are sporadic, which means they occur in people without any known risk factors or gene mutations. In rare circumstances, prion diseases also can be transmitted by exposure to prion-contaminated tissues or other biological materials obtained from individuals with prion disease.<efsa>It could be transmitted by Five cases of atypical BSE were reported in cattle across the and five more reported by countries. A total of 721 cases of scrapie were detected in small ruminants in the 27 Member States and in the United Kingdom in respect of Northern Ireland: 538 in sheep (557 in 2022) and 183 in goats (224 in 2022).Surveillance of TSE in cervids is voluntary in the. Only Norway confirmed one case of Chronic Wasting Disease (one wild European moose)</efsa>.The PRNP gene provides the instructions to make a protein called the prion protein (PrP). Under normal circumstances, this protein may be involved in transporting copper into cells. The protein may also be involved in protecting brain cells and helping them communicate.[7][8]

Protein-only hypothesis

Protein could be the infectious agent, inducing its own replication by causing conformational change of normal cellular PrPC into PrPSc. Evidence for this hypothesis:

  • Infectivity titre correlates with PrPSc levels.
  • PrPSc is an isomer of PrPC
  • Denaturing PrP removes infectivity[9]
  • PrP-null mice cannot be infected[10]
  • PrPC depletion in the neural system of mice with established neuroinvasive prion infection reverses early spongeosis and behavioural deficits, halts further disease progression and increases life-span[11]

Multi-component hypothesis

While not containing a nucleic acid genome, prions may be composed of more than just a protein. Purified PrPC appears unable to convert to the infectious PrPSc form, unless other components are added, such as RNA and lipids.[12] These other components, termed cofactors, may form part of the infectious prion, or they may serve as catalysts for the replication of a protein-only prion.

Spread

Prions appear to be most infectious by direct contact with affected tissues. For example, Creutzfeldt–Jakob disease has been transmitted by taking injections of growth hormone harvested from human pituitary glands, from cadaver dura allografts, and from instruments used for brain surgery (prions can survive the "autoclave" sterilization process used for most surgical instruments). Eating affected animals can also spread the disease, especially with cannibalism or similar practices. An example is kuru, which reached epidemic proportions in the mid-20th century in the Fore people of Papua New Guinea, who used to consume their dead as a funerary ritual.[13] Laws in developed countries now ban the use of rendered ruminant proteins in ruminant feed as a precaution against the spread of prion infection in cattle and other ruminants.

Pathophysiology

Prion diseases are characterized by four features: spongiform change (the presence of many small holes), the death of neurons, astrocytosis (abnormal increase in the number of astrocytes due to the destruction of nearby neurons), and amyloid plaque formation. The recognition of these similarities prompted the first attempts to transmit a human prion disease (kuru) to a primate in 1966, followed by CJD in 1968 and GSS in 1981. These neuropathological features have formed the basis of the histological diagnosis of prion diseases, although it was recognized that these changes are variable from case to case and within the central nervous system in individual cases.[14]

Diagnosis

There continues to be a very practical problem with diagnosis of prion diseases, including BSE and CJD. They have an incubation period of months to decades during which there are no symptoms, even though the pathway of converting the normal brain PrP protein into the toxic, disease-related PrPSc form has started. At present, there is virtually no way to detect PrPSc reliably except by examining the brain using neuropathological and immunohistochemical methods after death. Accumulation of the abnormally folded PrPSc form of the PrP protein is a characteristic of the disease, but it is present at very low levels in easily accessible body fluids like blood or urine. Researchers have tried to develop methods to measure PrPSc, but there are still no fully accepted methods for use in materials such as blood.[citation needed]

In 2010, a team from New York described detection of PrPSc even when initially present at only one part in a hundred billion (10−11) in brain tissue. The method combines amplification with a novel technology called Surround Optical Fiber Immunoassay (SOFIA) and some specific antibodies against PrPSc. After amplifying and then concentrating any PrPSc, the samples are labelled with a fluorescent dye using an antibody for specificity and then finally loaded into a micro-capillary tube. This tube is placed in a specially constructed apparatus so that it is totally surrounded by optical fibres to capture all light emitted once the dye is excited using a laser. The technique allowed detection of PrPSc after many fewer cycles of conversion than others have achieved, substantially reducing the possibility of artefacts, as well as speeding up the assay. The researchers also tested their method on blood samples from apparently healthy sheep that went on to develop scrapie. The animals' brains were analysed once any symptoms became apparent. The researchers could therefore compare results from brain tissue and blood taken once the animals exhibited symptoms of the diseases, with blood obtained earlier in the animals' lives, and from uninfected animals. The results showed very clearly that PrPSc could be detected in the blood of animals long before the symptoms appeared.[15][16]

Types

Differences in shape between the different prion protein forms are poorly understood.

Prion diseases
ICTVdb Code[17] Disease name Natural host Prion name PrP isoform
Humans
90.001.0.01.007. Kuru Humans Kuru prion PrPKuru
90.001.0.01.008. Creutzfeldt–Jakob disease (CJD) CJD prion PrPsCJD
Variant Creutzfeldt–Jakob disease (vCJD, nvCJD) vCJD prion[18] PrPvCJD
90.001.0.01.009. Gerstmann-Sträussler-Scheinker syndrome (GSS) GSS prion PrPGSS
90.001.0.01.010. Fatal familial insomnia (FFI) FFI prion PrPFFI
Familial spongiform encephalopathy[19]
Other mammals
90.001.0.01.001. Scrapie Sheep and goats Scrapie prion PrPSc
90.001.0.01.002. Transmissible mink encephalopathy (TME) Mink TME prion PrPTME
90.001.0.01.003. Chronic wasting disease (CWD) Elk, white-tailed deer, mule deer and red deer CWD prion PrPCWD
90.001.0.01.004. Bovine spongiform encephalopathy (BSE)
commonly known as "mad cow disease" 		Cattle BSE prion PrPBSE
90.001.0.01.005. Feline spongiform encephalopathy (FSE) Cats FSE prion PrPFSE
90.001.0.01.006. Exotic ungulate encephalopathy (EUE) Nyala and greater kudu EUE prion PrPEUE
Camel spongiform encephalopathy (CSE)[20] Camel PrPCSE

Differential

Note that not all encephalopathies are caused by prions, as in the cases of PML (caused by the JC virus), CADASIL (caused by abnormal NOTCH3 protein activity), and Krabbe disease (caused by a deficiency of the enzyme galactosylceramidase). Progressive spongiform leukoencephalopathy (PSL)—which is a spongiform encephalopathy—is also probably not caused by a prion, although the adulterant that causes it among heroin smokers has not yet been identified.[21][22][23][24] This, combined with the highly variable nature of prion disease pathology, is why a prion disease cannot be diagnosed based solely on a patient's symptoms.

Treatment

There are no known cures for prion disease.[25] Treatment is generally supportive care.A number of medications are being studied to try to slow disease progression.[26]

Epidemiology

They are very rare but have reach epidemic proportions in certain populations. It is very hard to map the spread of the disease due to the difficulty of identifying individual strains of the prions. This means that, if animals at one farm begin to show the disease after an outbreak on a nearby farm, it is very difficult to determine whether it is the same strain affecting both herds—suggesting transmission—or if the second outbreak came from a completely different source.

Classic Creutzfeldt-Jakob disease (CJD) was discovered in 1920. It occurs sporadically over the world but is very rare. It affects about one person per million each year. Typically, the cause is unknown for these cases. It has been found to be passed on genetically in some cases. 250 patients contracted the disease through iatrogenic transmission (from use of contaminated surgical equipment).[27] This was before equipment sterilization was required in 1976, and there have been no other iatrogenic cases since then. In order to prevent the spread of infection, the World Health Organization created a guide to tell health care workers what to do when CJD appears and how to dispose of contaminated equipment.[28] The Centers for Disease Control and Prevention (CDC) have been keeping surveillance on CJD cases, particularly by looking at death certificate information.[29]

Chronic wasting disease (CWD) is a prion disease found in North America in deer and elk. The first case was identified as a fatal wasting syndrome in the 1960s. It was then recognized as a transmissible spongiform encephalopathy in 1978. Surveillance studies showed the endemic of CWD in free-ranging deer and elk spread in northeastern Colorado, southeastern Wyoming and western Nebraska. It was also discovered that CWD may have been present in a proportion of free-ranging animals decades before the initial recognition. In the United States, the discovery of CWD raised concerns about the transmission of this prion disease to humans. Many apparent cases of CJD were suspected transmission of CWD, however the evidence was lacking and not convincing.[30]

In the 1980s and 1990s, bovine spongiform encephalopathy (BSE or "mad cow disease") spread in cattle at an epidemic rate. The total estimated number of cattle infected was approximately 750,000 between 1980 and 1996. This occurred because the cattle were fed processed remains of other cattle. Then human consumption of these infected cattle caused an outbreak of the human form CJD. There was a dramatic decline in BSE when feeding bans were put in place. On May 20, 2003, the first case of BSE was confirmed in North America. The source could not be clearly identified, but researchers suspect it came from imported BSE-infected cow meat. In the United States, the USDA created safeguards to minimize the risk of BSE exposure to humans.[31]

Variant Creutzfeldt-Jakob disease (vCJD) was discovered in 1996 in England. There is strong evidence to suggest that vCJD was caused by the same prion as bovine spongiform encephalopathy.[32] A total of 231 cases of vCJD have been reported since it was first discovered. These cases have been found in a total of 12 countries with 178 in the United Kingdom, 27 in France, five in Spain, four in Ireland, four in the United States, three in the Netherlands, three in Italy, two in Portugal, two in Canada, and one each in Japan, Saudi Arabia, and Taiwan.[33]

History

In the 5th century BCE, Hippocrates described a disease like TSE in cattle and sheep, which he believed also occurred in humans.[34] Publius Flavius Vegetius Renatus records cases of a disease with similar characteristics in the 4th and 5th centuries AD.[35] In 1755, an outbreak of scrapie was discussed in the British House of Commons and may have been present in Britain for some time before that.[36] Although there were unsupported claims in 1759 that the disease was contagious, in general it was thought to be due to inbreeding and countermeasures appeared to be successful. Early-20th-century experiments failed to show transmission of scrapie between animals, until extraordinary measures were taken such as the intra-ocular injection of infected nervous tissue. No direct link between scrapie and human disease was suspected then or has been found since. TSE was first described in humans by Alfons Maria Jakob in 1921.[37] Daniel Carleton Gajdusek's discovery that Kuru was transmitted by cannibalism accompanied by the finding of scrapie-like lesions in the brains of Kuru victims strongly suggested an infectious basis to TSE.[38] A paradigm shift to a non-nucleic infectious entity was required when the results were validated with an explanation of how a prion protein might transmit spongiform encephalopathy.[39] Not until 1988 was the neuropathology of spongiform encephalopathy properly described in cows.[40] The alarming amplification of BSE in the British cattle herd heightened fear of transmission to humans and reinforced the belief in the infectious nature of TSE. This was confirmed with the identification of a Kuru-like disease, called new variant Creutzfeldt–Jakob disease, in humans exposed to BSE.[41] Although the infectious disease model of TSE has been questioned in favour of a prion transplantation model that explains why cannibalism favours transmission,[42] the search for a viral agent was, as of 2007, being continued in some laboratories.[43][44]

See also

References

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  2. ↑ 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 2.11 2.12 2.13 2.14 2.15 2.16 2.17 2.18 "Transmissible Spongiform Encephalopathies". National Institute of Neurological Disorders and Stroke. Archived from the original on 23 April 2023. Retrieved 23 April 2023. Archived 23 April 2023 at the Wayback Machine
  3. ↑ 3.0 3.1 3.2 3.3 3.4 3.5 3.6 3.7 "About Prion Diseases". Prion Diseases. CDC. 22 April 2024. Archived from the original on 19 March 2025. Retrieved 18 March 2025. Archived 19 March 2025 at the Wayback Machine
  4. ↑ Ironside, JW; Ritchie, DL; Head, MW (2017). "Prion diseases". Handbook of clinical neurology. 145: 393–403. doi:10.1016/B978-0-12-802395-2.00028-6. PMID 28987186.
  5. ↑ 5.0 5.1 "About Variant Creutzfeldt-Jakob Disease (vCJD)". Variant Creutzfeldt-Jakob Disease (vCJD). CDC. 12 November 2024. Archived from the original on 3 March 2025. Retrieved 18 March 2025. Archived 3 March 2025 at the Wayback Machine
  6. ↑ "Prion & PLPs Decontamination Options | UMN University Health & Safety". hsrm.umn.edu. University of Minnesota. Archived from the original on 14 June 2024. Retrieved 18 March 2025. Archived 14 June 2024 at the Wayback Machine
  7. ↑ Sakudo, Akikazu; Lee, Deug-chan; Saeki, Keiichi; Nakamura, Yuko; Inoue, Keiichi; Matsumoto, Yoshitsugu; Itohara, Shigeyoshi; Onodera, Takashi (2003). "Impairment of superoxide dismutase activation by N-terminally truncated prion protein (PrP) in PrP-deficient neuronal cell line". Biochemical and Biophysical Research Communications. 308 (3): 660–667. doi:10.1016/s0006-291x(03)01459-1. ISSN 0006-291X. PMID 12914801.
  8. ↑ Collinge, John; Whittington, Miles A.; Sidle, Katie C. L.; Smith, Corinne J.; Palmer, Mark S.; Clarke, Anthony R.; Jefferys, John G. R. (1994). "Prion protein is necessary for normal synaptic function". Nature. 370 (6487): 295–297. Bibcode:1994Natur.370..295C. doi:10.1038/370295a0. ISSN 1476-4687. PMID 8035877. Archived from the original on 2024-08-23. Retrieved 2025-02-17. Archived 2024-08-23 at the Wayback Machine
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  10. ↑ Sakudo A; Lee DC; Saeki K; et al. (August 2003). "Impairment of superoxide dismutase activation by N-terminally truncated prion protein (PrP) in PrP-deficient neuronal cell line". Biochemical and Biophysical Research Communications. 308 (3): 660–7. doi:10.1016/S0006-291X(03)01459-1. PMID 12914801.
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  12. ↑ Deleault NR, Harris BT, Rees JR, Supattapone S (June 2007). "Formation of native prions from minimal components in vitro". Proceedings of the National Academy of Sciences of the United States of America. 104 (23): 9741–6. Bibcode:2007PNAS..104.9741D. doi:10.1073/pnas.0702662104. PMC 1887554. PMID 17535913.
  13. ↑ Collins S, McLean CA, Masters CL (2001). "Gerstmann-Straussler-Scheinker syndrome, fatal familial insomnia, and kuru: a review of these less common human transmissible spongiform encephalopathies". J Clin Neurosci. 8 (5): 387–97. doi:10.1054/jocn.2001.0919. PMID 11535002. S2CID 31976428.
  14. ↑ Jeffrey M, Goodbrand IA, Goodsir CM (1995). "Pathology of the transmissible spongiform encephalopathies with special emphasis on ultrastructure". Micron. 26 (3): 277–98. doi:10.1016/0968-4328(95)00004-N. PMID 7788281.
  15. ↑ "Detecting Prions in Blood" (PDF). Microbiology Today: 195. August 2010. Archived from the original (PDF) on 2012-03-31. Retrieved 2011-08-21. Archived 2011-10-01 at the Wayback Machine
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  18. ↑ Believed to be identical to the BSE prion.
  19. ↑ Nitrini R, Rosemberg S, Passos-Bueno MR, da Silva LS, Iughetti P, Papadopoulos M, Carrilho PM, Caramelli P, Albrecht S, Zatz M, LeBlanc A (August 1997). "Familial spongiform encephalopathy associated with a novel prion protein gene mutation". Annals of Neurology. 42 (2): 138–46. doi:10.1002/ana.410420203. PMID 9266722. S2CID 22600579.
  20. ↑ "Deux chercheurs algériens découvrent la maladie du "chameau fou" à Ouargla". 2018-05-09. Archived from the original on 2018-06-17. Retrieved 2019-03-13. Archived 2018-06-17 at the Wayback Machine
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  25. ↑ "Therapeutic Approaches for Prion Diseases | NIAID: National Institute of Allergy and Infectious Diseases". www.niaid.nih.gov. 2019-10-21. Archived from the original on 2016-09-18. Retrieved 2024-07-17. Archived 2016-09-18 at the Wayback Machine
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  28. ↑ "Infection Control | Creutzfeldt-Jakob Disease, Classic (CJD) | Prion Disease | CDC". www.cdc.gov. Archived from the original on 2017-12-01. Retrieved 2017-11-09. Archived 2017-12-01 at the Wayback Machine
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  32. ↑ "Variant Creutzfeldt-Jakob disease". World Health Organization. Archived from the original on December 20, 2002. Retrieved 2017-11-09. Archived 2016-02-04 at the Wayback Machine
  33. ↑ "Risk for Travelers | Variant Creutzfeldt-Jakob Disease, Classic (CJD) | Prion Disease". www.cdc.gov. Archived from the original on 2017-12-01. Retrieved 2017-11-09. Archived 2017-12-01 at the Wayback Machine
  34. ↑ McAlister, V (June 2005). "Sacred disease of our times: failure of the infectious disease model of spongiform encephalopathy". Clin Invest Med. 28 (3): 101–4. PMID 16021982. Archived from the original on 2014-11-02. Retrieved 2011-06-20. Archived 2014-11-02 at the Wayback Machine
  35. ↑ Digesta Artis Mulomedicinae, Publius Flavius Vegetius Renatus
  36. ↑ Brown P, Bradley R; Bradley (December 1998). "1755 and all that: a historical primer of transmissible spongiform encephalopathy". BMJ. 317 (7174): 1688–92. doi:10.1136/bmj.317.7174.1688. PMC 1114482. PMID 9857129.
  37. ↑ Katscher F. (May 1998). "It's Jakob's disease, not Creutzfeldt's". Nature. 393 (6680): 11. Bibcode:1998Natur.393Q..11K. doi:10.1038/29862. PMID 9590681. S2CID 205000018.
  38. ↑ Gajdusek DC (Sep 1977). "Unconventional viruses and the origin and disappearance of kuru". Science. 197 (4307): 943–60. Bibcode:1977Sci...197..943C. doi:10.1126/science.142303. PMID 142303.
  39. ↑ Collins SJ, Lawson VA, Masters CL.; Lawson; Masters (Jan 2004). "Transmissible spongiform encephalopathies". Lancet. 363 (9204): 51–61. doi:10.1016/S0140-6736(03)15171-9. PMID 14723996. S2CID 23212525.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  40. ↑ Hope J, Reekie LJ, Hunter N, Multhaup G, Beyreuther K, White H, Scott AC, Stack MJ, Dawson M, Wells GA.; Reekie; Hunter; Multhaup; Beyreuther; White; Scott; Stack; Dawson; et al. (Nov 1988). "Fibrils from brains of cows with new cattle disease contain scrapie-associated protein". Nature. 336 (6197): 390–2. Bibcode:1988Natur.336..390H. doi:10.1038/336390a0. PMID 2904126. S2CID 4351199.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  41. ↑ Will RG, Ironside JW, Zeidler M, Cousens SN, Estibeiro K, Alperovitch A, Poser S, Pocchiari M, Hofman A, Smith PG.; Ironside; Zeidler; Cousens; Estibeiro; Alperovitch; Poser; Pocchiari; Hofman; Smith (April 1996). "A new variant of Creutzfeldt–Jakob disease in the UK". Lancet. 347 (9006): 921–5. doi:10.1016/S0140-6736(96)91412-9. PMID 8598754. S2CID 14230097.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  42. ↑ McAlister, V (June 2005). "Sacred disease of our times: failure of the infectious disease model of spongiform encephalopathy". Clin Invest Med. 28 (3): 101–4. PMID 16021982. Archived from the original on 2014-11-02. Retrieved 2011-06-20. Archived 2014-11-02 at the Wayback Machine
  43. ↑ Manuelidis L, Yu ZX, Barquero N, Banquero N, Mullins B; Yu; Banquero; Mullins (February 2007). "Cells infected with scrapie and Creutzfeldt–Jakob disease agents produce intracellular 25-nm virus-like particles". Proceedings of the National Academy of Sciences of the United States of America. 104 (6): 1965–70. Bibcode:2007PNAS..104.1965M. doi:10.1073/pnas.0610999104. PMC 1794316. PMID 17267596.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  44. ↑ "Infectious Particles". Manuelidis Lab. Archived from the original on 2019-06-20. Retrieved 2025-02-17. Archived 2019-06-20 at the Wayback Machine

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