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Categories: Biology: Microbiology, Engineering: Biometric

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Scientists have determined that a plant protein involved in the timing of flowering could in fact be a prion. This is the first time that a possible prion has been identified in plants, and it may play a role in a plant's 'memory' of cold exposure during winter.

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Transmissible spongiform encephalopathies (TSEs), or prion diseases, are a family of rare progressive, neurodegenerative illnesses that affect both humans and animals. TSE surveillance is important for public health and food safety because TSEs have the potential of crossing from animals to humans, as seen with the spread of mad cow disease, or bovine spongiform encephalopathy (BSE). A new study describes an advanced assay that offers better sensitivity than currently available tests for detecting a prion disease affecting elk.

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Rabbits have long been considered immune to prion disease, but recently scientists have shown that they can -- under certain circumstances -- get transmissible spongiform encephalopathy (or TSE, the scientific term for the fatal brain disease caused by prions). Two studies address what makes rabbits hard to infect with prions and how their resistance can be overcome.

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Prions are fascinating, enigmatic, and might teach us not only about rare prion diseases like Creutzfeld-Jakob disease, mad cow disease, or scrapie, but also about other more common neurodgenerative diseases. Two studies report progress with novel tools and paradigms to study prion disease.

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Grass plants can bind, uptake and transport infectious prions, according to researchers. Prions are the protein-based infectious agents responsible for a group of diseases called transmissible spongiform encephalopathy, which includes bovine spongiform encephalopathy (mad cow disease) in cattle, scrapie in sheep, variant Creutzfeldt-Jakob disease in humans and chronic wasting disease (CWD) in deer, elk and moose. All are fatal brain diseases with incubation periods that last years.

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Chronic wasting disease (CWD) affects North American elk and deer, but has not been observed in humans. Using a mouse model that expresses an altered form of the normal human prion protein, researchers have determined why the human proteins aren’t corrupted when exposed to the elk prions. Their study identifies a small loop in the human prion protein that confers resistance to chronic wasting disease.

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The pathogens responsible for scrapie in small ruminants (prions) have the potential to convert the human prion protein from a healthy state to a pathological state, researchers have discovered for the first time. In mice models reproducing the human species barrier, this prion induces a disease similar to Creutzfeldt-Jakob disease. These primary results stress the necessity to reassess the transmission of this disease to humans.   

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Researchers say that a vaccination they have developed to fight a brain-based, wasting syndrome among deer and other animals may hold promise on two additional fronts: protecting US livestock from contracting the disease, and preventing similar brain infections in humans.

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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.