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Categories: Biology: Microbiology, Space: General

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The misfolded and infectious prion protein that is a marker for variant Creutzfeldt-Jakob disease – linked to the consumption of infected cattle meat – has been detected in the urine of patients with the disease. Variant Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy in animals – also known as Mad Cow disease – are fatal neurodegenerative disorders. There are currently no noninvasive tools available to diagnose the disease and there are no treatments.

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The first cases of mad cow disease in humans occurred in the late 1990s and are thought to be the consequence of eating contaminated beef products. Several cases of secondary infections caused by transfusions with blood from donors who developed vCJD have been reported, raising concerns about the safety of blood products. A new article describes an assay that can detect prions in blood samples from humans with vCJD and in animals at early stages of the incubation phase.

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Transmission of prions between species is inefficient, and only a small proportion of exposed recipients become sick within their lifetimes. A new study takes a close look at one exception to this rule: bank voles appear to lack a species barrier for prion transmission, and their universal susceptibility turns out to be both informative and useful for the development of strategies to prevent prion transmission.

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A blood test accurately screened for infection with the agent responsible for variant Creutzfeldt-Jakob disease (vCJD), a fatal neurological disease. vCJD is a fatal degenerative brain disorder thought to be caused by a misfolded protein (prion) in the brain and contracted most commonly through eating infected beef. Up to 3 million cattle in the United Kingdom may have been infected with BSE (bovine spongiform encephalopathy), and establishing accurate prevalence estimates through screening for vCJD infection would guide public health initiatives.

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A new study published shows similarities in the pathogenesis of prion disease -- misfolded proteins that can lead to neurological diseases -- and the HIV virus.

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Prions are unique infective agents -- unlike viruses, bacteria, fungi and other parasites, prions do not contain either DNA or RNA. Despite their seemingly simple structure, they can propagate their pathological effects like wildfire, by "infecting" normal proteins. PrPSc (the pathological form of the prion protein) can induce normal prion proteins (PrPC) to acquire the wrong conformation and convert into further disease-causing agents.

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New research has uncovered a quality control mechanism in brain cells that may help keep deadly neurological diseases in check for months or years.

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Chronic wasting disease, the deer-equivalent of mad cow disease, has crept across the US landscape from west to east, and was first detected in the Midwest in 2002. Little is known about its potential to infect humans. Now researchers offer a first look at the long-term effectiveness of the practice of culling deer in areas affected by CWD to keep the disease in check.

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By directly altering the gene coding for the prion protein (PrP), researchers have created mouse models of two neurodegenerative prion diseases, each of which manifests in different regions of the brain. These new models for fatal familial insomnia (FFI) and Creutzfeldt-Jakob disease (CJD) accurately reflect the distinct patterns of destruction caused by the these diseases in humans.

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Prion proteins are the infectious pathogens that cause Mad Cow Disease and Creutzfeldt-Jakob disease. They occur when a normal prion protein becomes deformed and clumped. The naturally occurring prion protein is harmless and can be found in most organisms. In humans, it is found in our brain cell membrane. By contrast, the abnormally deformed prion protein is poisonous for the brain cells. Scientists have now discovered that the prion protein has a kind of switch that controls its toxicity.

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The key to treating neurodegenerative prion diseases such as mad cow disease and Creutzfeldt-Jakob disease may lie in the ribosome, the protein synthesis machinery of the cell. Prion diseases are fatal neurodegenerative diseases caused by misfolding of prion proteins. Examples of prion diseases are scrapie in sheep, mad cow disease and Creutzfeldt-Jakob disease in human.

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Scientists have for the first time identified a pair of drugs already approved for human use that show anti-prion activity and, for one of them, great promise in treating rare and universally fatal disorders, such as Creutzfeldt-Jakob disease, caused by misfolded proteins called prions.

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A team of scientists has added markedly to the job description of prions as agents of change, identifying a prion capable of triggering a transition in yeast from its conventional single-celled form to a cooperative, multicellular structure. This change, which appears to improve yeast's chances for survival in the face of hostile environmental conditions, is an epigenetic phenomenon -- a heritable alteration brought about without any change to the organism’s underlying genome.

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An iron imbalance caused by prion proteins collecting in the brain is a likely cause of cell death in Creutzfeldt-Jakob disease, researchers have found. The breakthrough follows discoveries that certain proteins found in the brains of Alzheimer's and Parkinson's patients also regulate iron.

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Medical researchers have made a discovery that may explain how prion diseases, like chronic wasting disease and mad cow disease, adapt in order to spread between various types of animals.

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Researchers have shown that neuro-inflammation plays a crucial role in initiating prion disease.

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Crows fed on prion-infected brains from mice can transmit these infectious agents in their feces and may play a role in the geographic spread of diseases caused by prions, such as chronic wasting disease or scrapie.

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A simple blood test for Creutzfeldt-Jakob Disease and Mad Cow disease is a step closer, following a breakthrough by medical researchers in Australia.

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Many of us are familiar with prion disease from its most startling and unusual incarnations —- the outbreaks of “mad cow” disease (bovine spongiform encephalopathy) that created a crisis in the global beef industry. Or the strange story of Kuru, a fatal illness affecting a tribe in Papua New Guinea known for its cannibalism. Both are forms of prion disease, caused by the abnormal folding of a protein and resulting in progressive neurodegeneration and death.

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Researchers have identified a new class of compounds that inhibit the spread of prions, misfolded proteins in the brain that trigger lethal neurodegenerative diseases in humans and animals. Scientists have now developed compounds that clear prions from infected cells derived from the brain.