The mad cow crisis is a health and socio-economic crisis characterized by the collapse of beef consumption in the 1990s, as consumers became concerned about the transmission of bovine spongiform encephalopathy (BSE) to humans through the ingestion of this type of meat.
Background BSE is a degenerative infection of the central nervous system in cattle. It is a fatal disease, similar to scrapie in sheep and goats, caused by a prion. A major epizootic affected the UK, and to a lesser extent a number of other countries, between 1986 and the 2000s, infecting more than 190,000 animals, not counting those that remained undiagnosed. The epidemic is thought to have originated in the feeding of cattle with meat and bone meal, obtained from the uneaten parts of cattle and animal cadavers. The epidemic took a particular turn when scientists realized in 1996 that the disease could be transmitted to humans through the consumption of meat products. As of 24 January 2017, the disease had claimed 223 human victims worldwide (including 177 in the UK and 27 in France) affected by symptoms similar to Creutzfeldt-Jakob disease, a disease of the same nature as BSE. Communicated to the general public by the media, the crisis erupted in 1996. It involved both ethical aspects, with consumers becoming aware of certain practices that were common in livestock farming but of which they had been unaware, such as the use of meat and bone meal, and economic aspects, with the ensuing fall in beef consumption and the cost of the various measures adopted. Various measures were taken to curb the epidemic and safeguard human health, including a ban on the use of meat and bone meal in cattle feed, the withdrawal from consumption of products considered to be at risk, and even of certain animals (animals over 30 months of age in the UK), screening for the disease in slaughterhouses, and the systematic slaughter of herds where a sick animal had been observed. Nowadays, the epidemic is almost completely under control, despite 37 bovine cases still being diagnosed in the UK in 2008. On 23 March 2016, a new case of mad cow disease was detected in France in the Ardennes department. This is the third isolated case of BSE of this type detected in Europe since 2015.
Epidemiology
The disease was first identified in the United Kingdom in 1986.
Symptoms
BSE affects the brain and spinal cord of cattle. It causes brain lesions characterized by spongy changes visible under the light microscope, corresponding to vacuolated neurons. Neurons are lost to varying degrees, and astrocytes and microglia (brain cells with an immune function) multiply. Pathogens accumulate to form characteristic amyloid plaques, though these are less prevalent than in other transmissible spongiform encephalopathies. External symptoms generally appear 4 to 5 years after contamination, and always in animals over 2 years of age (generally between 3 and 7 years). Initially, they are manifested by a change in the animal's behavior (nervousness and aggressiveness), which may sometimes kick, show apprehension and hypersensitivity to external stimuli (noise, touch, dazzle), and isolate itself from the rest of the herd. Milk production and weight generally decrease, while appetite remains unchanged. Progression can last from a week to a year, with the different phases of the disease varying in duration from one animal to another. In the final stage of evolution, the animal has real locomotion problems. They frequently lose their balance, sometimes unable to stand up again. Physiologically, the animal is tachycardic and feverless. However, the appearance of these symptoms is not a sure sign of BSE. In fact, locomotor disorders such as grass tetany are common in cattle, making diagnosis of the disease difficult.
Nature of the pathogen The nature of the infectious agent remains debated. The leading theory is that a protein folds abnormally and becomes a prion, capable of causing other proteins to also fold incorrectly. A resistant form of the prion (PrPSc, also known as PrPRes, PrPD, or PrPBSE) accumulates in the brain, eventually leading to neuronal death and the formation of amyloid plaques. As a protein, the prion has no metabolism of its own, and is therefore resistant to freezing, desiccation and heat at normal cooking temperatures, even those reached for pasteurization and sterilization. To be destroyed, the prion must be heated to 133 °C for 20 minutes at 3 bars of pressure.
Origins of the epizootic The origins of the BSE pathogen are uncertain. Two hypotheses are widely supported. The first is that the disease originated through interspecific contamination from a closely related disease, scrapie, which affects sheep and goats. The possibility of interspecific transmission of scrapie has been proven experimentally, but the clinical and neuropathological disorders associated with the disease differ from those of bovine spongiform encephalopathy. This observation led to the formulation of a second hypothesis, according to which the disease is endemic to the bovine species, and very thinly spread before it was amplified in the mid-1980s. The description in an 1883 veterinary journal of a case of scrapie in a bovine is an argument used by advocates of this second theory, although this case may correspond to a completely different neurological disease. Numerous other more or less credible theories regularly enter the debate, with none really emerging.
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