Instruct: Given a question, retrieve passages that answer the question.
Query: Is Scrapie like Mad Cow Disease?
Prions are misfolded proteins which characterize several fatal neurodegenerative diseases in animals and humans.[1] It is not known what causes the normal protein to misfold; the abnormal 3-D structure is suspected to confer infectious properties. The word prion derives from "proteinaceous infectious particle".[2][3][4] Prions composed of the prion protein (PrP) are hypothesized as the cause of transmissible spongiform encephalopathies (TSEs),[5] including scrapie in sheep, chronic wasting disease (CWD) in deer, bovine spongiform encephalopathy (BSE) in cattle (commonly known as "mad cow disease"), and Creutzfeldt-Jakob disease (CJD) in humans.
camel spongiform encephalopathy commonly known as mad camel disease This disease, similar to mad cow disease, was discovered by two Algerian researchers, among them Dr Baaissa Babelhadj, veterinarian of the slaughter of the city of Ouargla in coordination with Italian researchers, This infection is a new form of prion disease and a type of Transmissible spongiform encephalopathy that affects for the first time non-ruminant mammals (camels) and is associated with mad cow disease in the characteristics of the ability to move to other animal species and to human consumers. 
Different hypotheses exist for the origin of BSE in cattle. One hypothesis suggests it may have jumped species from the disease scrapie in sheep, and another hypothesis suggests that it evolved from a rare spontaneous form of "mad cow disease" that has been seen occasionally in cattle for many centuries. In the 5th century BC, Hippocrates described a similar illness in cattle and sheep, which he believed also occurred in man. Publius Flavius Vegetius Renatus recorded cases of a disease with similar characteristics in the fourth and fifth centuries AD.
According to the prion theory, prions are infectious pathogens that do not contain nucleic acids. These abnormally folded proteins are found characteristically in some diseases such as scrapie, bovine spongiform encephalopathy (mad cow disease) and Creutzfeldt–Jakob disease.
"With scrapie, the archetypical TSE, which is a natural disease in sheep and goats, the disease can appear suddenly in a flock in the absence of any known exposure to infected flocks (Palsson, 1979). Finally, fields in Iceland, that were left empty for up to 3 years after the destruction of scrapie-infected flocks, were repopulated with known scrapie-free sheep, and some of the sheep in this latter group subsequently developed scrapie (Palsson, 1979). This last 'experiment in nature' has yielded similar results a number of times in Iceland and in the United Kingdom. In one Icelandic farm, flocks have been eradicated three times; each time, the farm was left without sheep for 2 years, and after restocking with sheep from scrapie-free areas, the disease reappeared. Several years ago, a suggestion was made (S Sigurdarson, personal communication) that hay mites would be a good candidate as a vector for scrapie; this led to infection of mice with mite samples prepared from hay obtained from five Icelandic farms. Ten of these 71 mice became sick after injection with mite preparations from three of the five farms (Wisniewski et al, 1996; Rubenstein et al, 1998). The incubation periods ranged from 340 days to 626 days, and these mice had the protease-resistant form PrpSc, of a host-coded glycoprotein, PrPc . The protease-resistant form is a marker of TSE disease (Prusiner, 1991; Parchi et al, 1996). For some of these clinically positive mice, the banding pattern on WB analysis was unique (Wisniewski et al, 1996; Rubenstein et al, 1998)."[45]
SOFIA has demonstrated its potential as a device with a wide range of applications. These include clinical applications, such as detecting diseases, discovering predispositions to pathologies, establishing a diagnosis and tracking the effectiveness of prescribed treatments, and nonclinical applications, such as preventing the entry of toxins and other pathogenic agents into products intended for human consumption:SOFIA has been used to rapidly detect the abnormal form of the prion protein (PrP) in samples of bodily fluids, such as blood or urine. PrP is the marker protein used in diagnostics for transmissible spongiform encephalopathies (TSEs), examples of which include bovine spongiform encephalopathy in cattle (i.e. “mad cow” disease), scrapie in sheep, and Creutzfeldt–Jakob disease in humans. Currently, no rapid means exists for the "ante mortem" detection of PrP in the dilute quantities in which it usually appears in bodily fluids. SOFIA has the advantages of requiring little sample preparation, and allowing for electronic diagnostic equipment to be placed outside the containment area.
Kuru was shown to have remarkable similarity to scrapie, a disease of sheep and goats caused by an unconventional infectious agent. Subsequently, additional human agents belonging to the same group were discovered. They include sporadic, familial, and variant Creutzfeldt–Jakob disease. Gajdusek recognized that diseases like Kuru and Creutzfeldt–Jakob disease were caused by a new infectious agent that had not yet been identified. Further research on the scrapie agent by Stanley Prusiner and others led to the identification of endogenous proteins called prions as the cause of these diseases.
Frank O. Bastian is an American medical doctor and biologist at Louisiana State University. He specializes in the transmissible spongiform encephalopathies (TSEs), which include, but are not limited to, Bovine spongiform encephalopathy (BSE) "Mad cow disease" in cattle, scrapie in sheep and goats, and Creutzfeldt–Jakob disease (CJD) in humans.
Examples of structural inheritance include the propagation of prions, the infectious proteins of diseases such as scrapie (in sheep and goats), bovine spongiform encephalopathy ('mad cow disease') and Creutzfeldt–Jakob disease (although the protein-only hypothesis of prion transmission has been considered contentious until recently). Prions based on heritable protein structure also exist in yeast. Structural inheritance has also been seen in the orientation of cilia in protozoans such as "Paramecium" and "Tetrahymena", and 'handedness' of the spiral of the cell in "Tetrahymena", and shells of snails. Some organelles also have structural inheritance, such as the centriole, and the cell itself (defined by the plasma membrane) may also be an example of structural inheritance. To emphasize the difference of the molecular mechanism of structural inheritance from the canonical Watson-Crick base pairing mechanism of transmission of genetic information, the term 'Epigenetic templating' was introduced.
Since 1998 and the mad cow epidemics, an EU directive forbids the production of "smalahove" from adult sheep, due to fear of the possibility of transmission of scrapie, a deadly, degenerative prion disease of sheep and goats, though scrapie does not appear to be transmissible to humans. It is now only allowed to be produced from the heads of lambs.
What do "mad cows", people with neurodegenerative diseases, and an unusual type of inheritance in yeast have in common? They are all experiencing the consequences of misfolded proteins. ... In humans the consequences can be deadly, leading to such devastating illnesses as Alzheimer's Disease. In one case, the misfolded protein is not only deadly to the unfortunate individual in which it has appeared, but it can apparently be passed from one individual to another under special circumstances – producing infectious neurodegenerative diseases such as mad-cow disease in cattle and Creutzfeldt–Jacob Disease in humans.
A control flock of Swaledales has been used to study and develop scrapie-resistant sheep. An infectious, persistent, and spontaneous disease, animals infected with scrapie must be quarantined and destroyed. The experimental breeding involved selecting a group of Swaledale sheep with low suspectability to the disease, injecting them with the agents of the disease, and breeding from the survivors. The research has concluded that the offspring of the infected sheep are more able to survive scrapie.
Bovine spongiform encephalopathy (BSE), commonly known as mad cow disease, is a neurodegenerative disease of cattle. Symptoms include abnormal behavior, trouble walking, and weight loss. Later in the course the cow becomes unable to move. The time between infection and onset of symptoms is generally four to five years. Time from onset of symptoms to death is generally weeks to months. Spread to humans is believed to result in variant Creutzfeldt–Jakob disease (vCJD). As of 2018 a total of 231 cases of vCJD have been reported globally.
BSE is due to an infection by a misfolded protein, known as a prion. Cattle are believed to have been infected by being fed meat-and-bone meal (MBM) that contained the remains of other cattle who spontaneously developed the disease or scrapie-infected sheep products. The outbreak increased throughout the United Kingdom due to the practice of feeding meat-and-bone meal to young calves of dairy cows. Cases are suspected based on symptoms and confirmed by examination of the brain. Cases are classified as classic or atypical, with the latter divided into H- and L types.
Efforts to prevent the disease in the UK include not allowing any animal older than 30 months to enter either the human food or animal feed supply. In Europe all cattle over 30 month must be tested if they will become human food. In North America tissue of concern, known as specified risk material, may not be added to animal feed or pet food. About 4.4 million cows were killed during the eradication program in the UK.
Four cases were reported globally in 2017 and the condition has been deemed to be nearly eradicated. In the United Kingdom, from 1986 to 2015, more than 184,000 cattle were diagnosed with the peak of new cases occurring in 1993. A few thousand additional cases have been reported in other regions of the world. It is believed that a few million cattle with the condition likely entered the food supply during the outbreak. 
The sale of the African variety of smokies is illegal in many western countries. Nevertheless, they are sometimes available on the black market in cities with large expatriate West African Muslim populations. This prohibition is largely due to fear of the possibility of transmission of scrapie and bovine spongiform encephalopathy (BSE, mad cow disease), deadly, degenerative prion diseases that are spread by ingestion of nerve and brain tissue from infected ungulates such as sheep, cows and goats. Furthermore, butchering an ungulate carcass with the skin intact and unsterilized considerably raises the risks for induction of fecal coliform bacteria such as "E. coli" or "Salmonella" into the meat and is thus banned in the UK by law. This risk is heightened because the smokies are generally produced in covert (and often grossly unsanitary) butchering facilities and handled without proper sanitary procedures. Furthermore, the goats and sheep used are traditionally old, worn-out or lame animals bought inexpensively from milk and wool farms and are not intended for human consumption.
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. 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. Not until 1988 was the neuropathology of spongiform encephalopathy 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.
Prions are infectious protein molecules that do not contain DNA or RNA. They can cause infections such as scrapie in sheep, bovine spongiform encephalopathy ("mad cow" disease) in cattle, and chronic wasting disease in deer; in humans, prionic diseases include Kuru, Creutzfeldt–Jakob disease, and Gerstmann–Sträussler–Scheinker syndrome.
Charles Weissmann (born 14 October 1931) is a Hungarian-born Swiss molecular biologist. Weissmann is particularly known for the first cloning and expression of interferon and his contributions to the unraveling of the molecular genetics of neurogenerative prion diseases such as scrapie, Creutzfeldt–Jakob disease and "mad cow disease".
After the first case of mad cow disease that was discovered, two more cases emerged. In 2005, the second instance was found in a cow in Texas, and the third was found in 2006 in a cow from Alabama. In 2012, this issue still remains a controversy. On April 24, 2012, the Department of Agriculture discovered a dairy cow in central California with mad cow disease. The USDA's chief veterinary officer, John Clifford, stated that the cow's meat did not enter the food supply. In addition to this, the carcass will be destroyed. The infected cow was found due to random sampling and is considered the fourth cow in the U.S. to be infected with BSE. This has caused the controversy to arise once again and speculation on whether the VSTA regulates testing for BSE in cows is still a hot topic to be discussed.
Prions are infectious pathogens that do not contain nucleic acids. Prions are abnormal proteins whose presence causes some diseases such as scrapie, bovine spongiform encephalopathy (mad cow disease), and Creutzfeldt–Jakob disease. The discovery of prion as a new class of pathogen allowed Stanley B. Prusiner to receive the Nobel Prize in Physiology or Medicine in 1997.
The prion gene that codes for the prion protein is highly conserved in most mammals, meaning the gene is similar and present in most species of mammals. Three locations on the prion protein gene have been identified as highly polymorphic and may have an effect on scrapie: codons 136, 154, and 171.[47] Codon 154 has not shown any evidence of having a high effect on scrapie susceptibility, but is most likely having an effect on incubation time of the disease. Codons 136 and 171 are thought to control the incubation time as well as the susceptibility of the disease, and are the ones the USDA uses in its breeding standard.[48][49][50] Codon 171 has been determined to be the major genetic factor in scrapie susceptibility.[51][52]
Scrapie is a fatal, degenerative disease that affects the nervous systems of sheep and goats.[1] It is one of several transmissible spongiform encephalopathies (TSEs), which also includes bovine spongiform encephalopathy (BSE or "mad cow disease"), Creutzfeldt-Jakob disease (CJD) in humans, and chronic wasting disease in deer. Like other spongiform encephalopathies, the cause of scrapie is unknown, but is thought to be caused by an infectious misfolded protein called a prion.[2][3] Scrapie has been known since 1732, and does not appear to be transmissible to humans.[4][5]
In March 2013, food inspectors found 57 tonnes of frozen sheepmeat at Spanghero, that had been imported from the United Kingdom and that included mechanically recovered meat (MSM). MSM is banned in the European Union, as it may contain fragments of bone. Bones of bovines, ovines or caprids may not be imported into EU countries from countries with a risk of spongiform encepalopathies; this includes the UK, following the mad cow disease outbreak of the 1990s, and the prevalence of scrapie among sheep there. Spanghero blamed its supplier Draap (the Dutch word for "horse" reversed) for false labelling.
Cattle diseases were in the center of attention in the 1980s and 1990s when the Bovine spongiform encephalopathy (BSE), also known as mad cow disease, was of concern. Cattle might catch and develop various other diseases, like blackleg, bluetongue, foot rot too.
The use of soil conservation practices such as crop rotation, cover crops, and windbreaks was expanded following the drought experiences of the dirty thirties. Literally layers and layers of topsoil would be blowing away during this time. Bow River Irrigation Project, Red Deer River Project and the St. Mary Irrigation project of Alberta, were a few of the major projects undertaken by the Prairie Farm Rehabilitation Act (P.F.R.A.) resulting in reservoirs, and distribution systems. A current project is soil liming at the Land Resource Research Institute.
Wheat diseases such as wheat bunt and stinking smut can be successfully treated with a fungicide.
Disease of plants and animals can break an agricultural producer. Tuberculosis in animals was an early threat, and cattle needed to be tested, and areas accredited in 1956. The newer disease such as chronic wasting disease or transmissible spongiform encephalopathy (TSE) affects both elk and deer. Elk and deer raising is a pioneer field of domestication, has had a setback with this disease. Mad cow disease in cattle and scrapie of sheep are monitored by the Canadian Food Inspection Agency. The poultry sector was plagued by Pullorum disease, and by controlling the flock via poultry husbandry, this disease has been brought under control.
TSEs 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.