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Transmissible spongiform encephalopathy

transmissible spongiform encephalopathy, transmissible spongiform encephalopathy symptoms
Transmissible spongiform encephalopathies TSEs, also known as prion diseases, are a group of progressive, invariably fatal, conditions that affect the brain encephalopathies and nervous system of many animals, including humans According to the most widespread hypothesis, they are transmitted by prions, though some other data suggest an involvement of a Spiroplasma infection Mental and physical abilities deteriorate and many tiny holes appear in the cortex causing it to appear like a sponge hence spongiform when brain tissue obtained at autopsy is examined under a microscope The disorders cause impairment of brain function, including memory changes, personality changes and problems with movement that worsen chronically

Prion diseases of humans include Creutzfeldt–Jakob disease—which has four main forms, the sporadic sCJD, the hereditary/familiar fCJD, the iatrogenic iCJD and the variant form vCJD—Gerstmann–Sträussler–Scheinker syndrome, fatal familial insomnia, kuru, and the recently discovered variably protease-sensitive prionopathy These conditions form a spectrum of diseases with overlapping signs and symptoms TSEs in non-human mammals include scrapie in sheep, bovine spongiform encephalopathy BSE—popularly known as 'mad cow's disease'—in cattle and chronic wasting disease CWD in deer and elk The variant form of Creutzfeldt–Jakob disease is caused by exposure to bovine spongiform encephalopathy prions

Unlike other kinds of infectious disease, which are spread by agents with a DNA or RNA genome such as virus or bacteria, the infectious agent in TSEs is believed to be a prion, thus being composed solely of protein material Misshapen prion proteins carry the disease between individuals and cause deterioration of the brain TSEs are unique diseases in that their aetiology may be genetic, sporadic, or infectious via ingestion of infected foodstuffs and via iatrogenic means eg, blood transfusion Most TSEs are sporadic and occur in an animal with no prion protein mutation Inherited TSE occurs in animals carrying a rare mutant prion allele, which expresses prion proteins that contort by themselves into the disease-causing conformation Transmission occurs when healthy animals consume tainted tissues from others with the disease In the 1980s and 1990s, bovine spongiform encephalopathy BSE spread in cattle in an epidemic fashion This occurred because cattle were fed the processed remains of other cattle, a practice now banned in many countries In turn, consumption by humans of bovine-derived foodstuff which contained prion-contaminated tissues resulted in an outbreak of the variant form of Creutzfeldt–Jakob disease in the 1990s and 2000s

Prions cannot be transmitted through the air or through touching or most other forms of casual contact However, they may be transmitted through contact with infected tissue, body fluids, or contaminated medical instruments Normal sterilization procedures such as boiling or irradiating materials fail to render prions non-infective


  • 1 Classification
  • 2 History
  • 3 Features
  • 4 Genetics
  • 5 Competing hypotheses
    • 51 Protein-only hypothesis
    • 52 Multi-component hypothesis
    • 53 Viral hypothesis
  • 6 Epidemiology
  • 7 Possible cure or vaccine and diagnosis
  • 8 See also
  • 9 Further reading
  • 10 References
  • 11 External links


Known spongiform encephalopathies
ICTVdb CodeDisease nameNatural hostPrion namePrP isoform
Non-human mammals
90001001001ScrapieSheep and goatsScrapie prionPrPSc
90001001002Transmissible mink encephalopathy TMEMinkTME prionPrPTME
90001001003Chronic wasting disease CWDElk, White-tailed deer, Mule Deer and Red DeerCWD prionPrPCWD
90001001004Bovine spongiform encephalopathy BSE
commonly known as "Mad Cow Disease"
CattleBSE prionPrPBSE
90001001005Feline spongiform encephalopathy FSECatsFSE prionPrPFSE
90001001006Exotic ungulate encephalopathy EUENyala and greater kuduEUE prionPrPEUE
Human diseases
90001001007KuruHumansKuru prionPrPKuru
90001001008Creutzfeldt–Jakob disease CJDCJD prionPrPsCJD
New Variant Creutzfeldt–Jakob disease vCJD, nvCJDvCJD prionPrPvCJD
90001001009Gerstmann-Sträussler-Scheinker syndrome GSSGSS prionPrPGSS
90001001010Fatal familial insomnia FFIFFI prionPrPFFI


In the 5th century BCE, Hippocrates described a disease like TSE in cattle and sheep, which he believed also occurred in man Publius Flavius Vegetius Renatus records cases of a disease with similar characteristics in the 4th and 5th centuries AD 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 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 disease in man was suspected then or has been found since TSE was first described in man by Alfons Maria Jakob in the 1921 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 The priority given the search for a viral infectious agent almost cost Stanley Prusiner tenure when his research showed that a protein transferred the disease 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 It wasn't until 1988 that the neuropathology of spongiform encephalopathy was properly described in cows 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 Although the infectious disease model of TSE has been questioned in favour of a prion transplantation model that explains why cannibalism favours transmission, the search for a viral agent is being continued in some laboratories


The degenerative tissue damage caused by human prion diseases CJD, GSS, and kuru is characterised by four features:spongiform change, neuronal loss, astrocytosis, and amyloid plaque formation These features are shared with prion diseases in animals, and 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 human prion diseases for many years, although it was recognized that these changes are enormously variable both from case to case and within the central nervous system in individual cases

The clinical signs in humans vary, but commonly include personality changes, psychiatric problems such as depression, lack of coordination, and/or an unsteady gait ataxia Patients also may experience involuntary jerking movements called myoclonus, unusual sensations, insomnia, confusion, or memory problems In the later stages of the disease, patients have severe mental impairment dementia and lose the ability to move or speak

Early neuropathological reports on human prion diseases suffered from a confusion of nomenclature, in which the significance of the diagnostic feature of spongiform change was occasionally overlooked The subsequent demonstration that human prion diseases were transmissible reinforced the importance of spongiform change as a diagnostic feature, reflected in the use of the term "spongiform encephalopathy" for this group of disorders

Prions appear to be most infectious when in direct contact with affected tissues For example, Creutzfeldt–Jakob disease has been transmitted to patients taking injections of growth hormone harvested from human pituitary glands, from cadaver dura allografts and from instruments used for brain surgery Brown, 2000 prions can survive the "autoclave" sterilization process used for most surgical instruments It is also believed that dietary consumption of affected animals can cause prions to accumulate slowly, especially when cannibalism or similar practices allow the proteins to accumulate over more than one generation 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 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

There exist evidence that prion diseases may be transmissible by the airborne route

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 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


Mutations in the PRNP gene cause prion disease 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

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 It may also be involved in protecting brain cells and helping them communicate 24 Point-Mutations in this gene cause cells to produce an abnormal form of the prion protein, known as PrPSc This abnormal protein builds up in the brain and destroys nerve cells, resulting in the signs and symptoms of prion disease

Familial forms of prion disease are inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder In most cases, an affected person inherits the altered gene from one affected parent

In some people, familial forms of prion disease are caused by a new mutation in the PRNP gene Although such people most likely do not have an affected parent, they can pass the genetic change to their children

Competing hypotheses

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 theory:

  • infectivity titre correlates with PrPSc levels However, this is disputed
  • PrPSc is an isomer of PrPC
  • Denaturing PrP removes infectivity
  • PrP-null mice cannot be infected
  • 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

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 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

Viral hypothesis

This hypothesis postulates that an infectious viral agent is the cause of the disease Evidence for this hypothesis is as follows:

  • Incubation time is comparable to a lentivirus
  • Strain variation of different isolates of PrPSc
  • An increasing titre of PrPSc as the disease progresses suggests a replicating agent


Transmissible spongiform encephalopathies TSE are very rare but can reach epidemic proportions 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 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 The Centers for Disease Control and Prevention CDC have been keeping surveillance on CJD cases, particularly by looking at death certificate information

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

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

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 231 total 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, 5 in Spain, 4 in Ireland, 4 in the United States, 3 in the Netherlands, 3 in Italy, 2 in Portugal, 2 in Canada, and one in Japan, Saudi Arabia, and Taiwan

Possible cure or vaccine and 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

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

Recent research from the University of Toronto and Caprion Pharmaceuticals has discovered one possible avenue that might lead to quicker diagnosis, a vaccine or possibly even treatment for prion diseases The abnormally folded proteins that cause the disease have been found to expose a side chain of amino acids that the properly folded protein does not expose Antibodies specifically coded to this side-chain amino acid sequence have been found to stimulate an immune response to the abnormal prions and leave the normal proteins intact

Another idea involves using custom peptide sequences Since some research suggests prions aggregate by forming beta barrel structures, work done in vitro has shown that peptides made up of beta barrel-incompatible amino acids can help break up accumulations of prion

A third idea concerns genetic therapy, whereby the gene for encoding protease-resistant protein is considered to be an error in several species, and therefore something to be inhibited

See also

  • Proteopathy
  • Prion

Further reading

  • Deadly Feasts:The "Prion" Controversy and the Public's Health, by Richard Rhodes
  • The Pathological Protein:Mad Cow, Chronic Wasting, and Other Deadly Prion Diseases, Phillip Yam, 2003, Springer, ISBN 0-387-95508-9
  • The Family That Couldn't Sleep by D T Max provides a history of prion diseases
  • Fatal Flaws:How a Misfolded Protein Baffled Scientists and Changed the Way We Look at the Brain, by Jay Ingram, 2012, HarperCollins Publishers


  • This entry incorporates public domain text originally from the National Institute of Neurological Disorders and Stroke, National Institutes of Healthand the US National Library of Medicine
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External links

  • Transmissible spongiform encephalopathy at Curlie based on DMOZ

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