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Mad cow disease

Bovine spongiform encephalopathy (BSE), commonly known as mad cow disease, is a fatal, neurodegenerative disease of cattle, which infects by a mechanism that shocked biologists on its discovery in late 20th century and appears transmissible to humans. While never having killed cattle on a scale comparable to other dreaded livestock diseases, such as foot and mouth and rinderpest, BSE has attracted wide attention because people assume humans can contract the disease, but it has never been proven that BSE has any link to variant Creutzfeld-Jakob disease (vCJD), sometimes called new variant Creutzfeld-Jakob disease (nvCJD), a human brain-wasting disease. more...

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Infectious agent

Unlike other kinds of infectious disease which are spread by microbes, the infectious agent in BSE is a specific type of protein. Misshapen ("misfolded") prion proteins carry the disease between individuals and cause deterioration of the brain. BSE is a type of transmissible spongiform encephalopathy (TSE). TSEs can arise in animals that carry a rare mutant prion allele, which expresses prions that contort by themselves into the disease-causing shape. Most TSEs, however, occur sporadically in animals that do not have a prion protein mutation. Transmission can occur when healthy animals consume tainted tissues from others with the disease. In the brain these proteins cause native cellular prion protein to deform into the infectious state which then goes on to deform further prion protein in an exponential cascade. These aggregate to form dense plaque fibers, which lead to the microscopic appearance of "holes" in the brain, degeneration of physical and mental abilities and ultimately death.

The BSE epidemic in British cattle

The British BSE epidemic in cattle was recognised in 1986. It was first believed to have originated in sheep, in which the related prion disease scrapie is common (such diseases collectively are called "transmissible spongiform encephalopathies" or TSEs). However, sheep and cattle TSEs are quite different and it is now thought more likely that BSE could have originated with a case of sporadic BSE in a single bovine. Prior to the BSE epidemic, cattle were fed with meat and bone meal, a high-protein substance obtained from the remnants of butchered animals, including cows and sheep. This practice allowed the accumulation of prions over many generations. As more animals became ill, more infectious tissue got into the feed, and so the number of cases reached epidemic proportions. The tissues that contain most of the pathogenic molecules are those of the brain and the nervous system, although infectious amounts have been shown experimentally to be present elsewhere, such as in blood.

The use of meat and bone meal as a protein supplement in cattle feed was widespread in Europe prior to about 1987. Soybean meal is the primary plant-based protein supplement fed to cattle. However, soybeans do not grow well in Europe, so cattle raisers throughout Europe turned to the less expensive animal byproduct feeds as an alternative. A change to the rendering process in the early 1980s may have resulted in a large increase of the infectious agents in the cattle feed. A contributing factor seems to have been lax British laws that did not require a high temperature sterilization of the protein meal. While other European countries like Germany required said animal byproducts to undergo a high temperature steam boiling process, this requirement had been eased in Britain as a measure to keep prices competitive.

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Blood test detects "mad cow" disease in hamsters
From Medical Laboratory Observer, 10/1/05

Blood test detects "mad cow" disease in hamsters. Three scientists at the University of Texas Medical Branch-Galveston have found a way to detect abnormal prion protein in blood samples from hamsters. If the test proves effective in cattle and humans, it could help determine the prevalence of the disease in the United States. "Mad cow" and related prion diseases are currently diagnosed only through the examination of brain tissue after death. Writing in Nature Medicine, Claudio Soto, Joaquin Castilla, and Paula Saa report that they have devised a way to stimulate a tiny, undetectable amount of abnormal prion protein in a blood sample to multiply so that it reaches detectable levels: "Our findings represent the first time that prions have been biochemically detected in blood."

At the end of August, Steve Sundlof, director of the Food and Drug Administration's Center for Veterinary Medicine, announced that the federal government was closing its investigation into the nation's first case of domestic "mad cow" disease. Investigators could not pin down how a Texas cow was infected and did not identify a specific food source as the likely cause of the animal's infection. According to Sundlof, the cow, which tested positive in June, likely ate contaminated food before the United States banned ground-up cattle remains in cattle feed in 1997.

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COPYRIGHT 2005 Gale Group

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