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Categories: Biology: Microbiology, Engineering: Biometric

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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.

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Bovine spongiform encephalopathy (BSE, or "mad cow disease") is a fatal disease in cattle that causes portions of the brain to turn sponge-like. This transmissible disease is caused by the propagation of a misfolded form of protein known as a prion, rather than by a bacterium or virus. Previous research has reported that the autonomic nervous system (ANS) becomes affected by the disease only after the central nervous system (CNS) has been infected. In a new study researchers found that the ANS can show signs of infection prior to involvement of the CNS.

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Toxic prions in the brain can be detected with self-illuminating polymers. The originators, at Linköping University in Sweden, has now shown that the same molecules can also render the prions harmless, and potentially cure fatal nerve-destroying illnesses.

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One of the greatest mysterious in cellular biology has been given a new twist. Researchers now show that prions, proteins that transmit heritable information without DNA or RNA, can contribute to drug resistance and cellular adaptation. Their discovery of a yeast prion with these properties demonstrates the active role of the prion conversion in cellular fitness adaptation, providing new insights into the potentially broader function of prions in living organisms.

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Scientists have identified a single prion protein that causes neuronal death similar to that seen in "mad cow" disease, but is at least 10 times more lethal than larger prion species.

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Scrapie is a neurodegenerative disease which can function as a model for other diseases caused by an accumulation of proteins resulting in tissue malformations (proteinpathies), such as Alzheimer's and Parkinson's disease. Many questions regarding these diseases still remain unanswered. A new study has uncovered a number of factors relating to the uptake of the prion protein (PrPSc) associated with the development of this disease and how this protein interacts with the immune cells in the intestines.

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Biochemists have identified a yeast protein called Lsb2 that can promote spontaneous prion formation. Prions can cause neurodegenerative disorders, such as mad cow/Creutzfeld-Jakob disease, in humans and animals.

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Researchers have identified an altered expression of endogenous retroviruses in BSE-infected macaques.

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Researchers have discovered two classes of yeast genes that may hold clues as to why proteins take on the misfolded prion form, a condition associated with several neurodegenerative diseases, such as "mad cow."