News tagged with prion
Scientists show 'lifeless' prions capable of evolutionary change and adaptation
Scientists from The Scripps Research Institute have determined for the first time that prions, bits of infectious protein devoid of DNA or RNA that can cause fatal neurodegenerative disease, are capable of Darwinian evolution.
Medicine & Health / Medical research
Dec 31, 2009 |
4.5 / 5 (31) |
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New study shows prions able to jump between species more easily than thought
(PhysOrg.com) -- A group of French researchers has found that prions are more easily able to jump between species than has been previously thought. In their paper published in Science, they show that prions ...
Jan 27, 2012 |
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Study points to disruption of copper regulation as key to prion diseases
(PhysOrg.com) -- An investigation of a rare, inherited form of Creutzfeldt-Jakob disease suggests that disrupted regulation of copper ions in the brain may be a key factor in this and other prion diseases.
Apr 17, 2009 |
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Unravelling the mystery of misfolding prions
(Phys.org) -- Researchers at the University of Alberta's physics department and the National Institute for Nanotechnology (NINT) are the first to map out the folding pathways of prions, malformed ...
May 30, 2012 |
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Research identifies drug target for prion diseases, 'mad cow'
Scientists at the University of Kentucky have discovered that plasminogen, a protein used by the body to break up blood clots, speeds up the progress of prion diseases such as mad cow disease.
Medicine & Health / Medical research
Jan 10, 2011 |
4.8 / 5 (5) |
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Scientists devise accelerated method to determine infectious prion strains
Current tests to identify specific strains of infectious prions, which cause a range of transmissible diseases (such as mad cow) in animals and humans, can take anywhere from six months to a year to yield results - a time-lag ...
Medicine & Health / Medical research
May 29, 2009 |
4.4 / 5 (5) |
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Dual role for immune cells in the brain
We all have at one time or another experienced the typical signs of an infection: the fever, the listlessness, the lack of appetite. They are orchestrated by the brain in response to circulating cytokines, ...
Medicine & Health / Neuroscience
Jan 13, 2010 |
4.4 / 5 (5) |
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Study shows infectious prions can arise spontaneously in normal brain tissue
In a startling new study that involved research on both sides of the Atlantic, scientists from The Scripps Research Institute in Florida and the University College London (UCL) Institute of Neurology in England have shown ...
Medicine & Health / Medical research
Jul 26, 2010 |
3.7 / 5 (6) |
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Common soil mineral degrades the nearly indestructible prion
(PhysOrg.com) -- In the rogues' gallery of microscopic infectious agents, the prion is the toughest hombre in town.
Biology /
Jan 14, 2009 |
5 / 5 (4) |
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A penny for your prions: Researchers study link between copper, mad cow disease
(PhysOrg.com) -- North Carolina State University researchers have discovered a link between copper and the normal functioning of prion proteins, which are associated with transmissible spongiform encephalopathy ...
Jun 25, 2009 |
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New sporadic prion protein disease identified
A new sporadic prion protein disease has been discovered. Variably protease-sensitive prionopathy (VPSPr), as it has been named, is the second type of complete sporadic disease to be identified since Creutzfeldt-Jakob disease ...
Medicine & Health / Neuroscience
Aug 13, 2010 |
4.8 / 5 (4) |
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Study Offers Evidence That Spongiform Brain Diseases Are Caused By Aberrant Protein
(PhysOrg.com) -- Scientists have determined how a normal protein can be converted into a prion, an infectious agent that causes fatal brain diseases in humans and mammals.
Medicine & Health / Medical research
Jan 28, 2010 |
4.3 / 5 (4) |
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Antibody key to treating variant CJD, scientists find
Scientists at the University of Liverpool have determined the atomic structure of the 'binding' between a brain protein and an antibody that could be key to treating patients with diseases such as variant CJD.
Medicine & Health / Diseases, Conditions, Syndromes
Mar 04, 2009 |
5 / 5 (3) |
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Eyes of cattle may become new windows to detect mad cow disease
The eyes may or may not be windows to the soul, as the old adage goes, but scientists are reporting evidence that a peek into the eyes of cattle may become the basis for a long-sought test to detect infection ...
Chemistry / Analytical Chemistry
Jun 02, 2010 |
5 / 5 (3) |
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BSE pathogens can be transmitted by air
Airborne prions are also infectious and can induce mad cow disease or Creutzfeldt-Jakob disorder. This is the surprising conclusion of researchers at the University of Zurich, the University Hospital Zurich and the University ...
Medicine & Health / Diseases, Conditions, Syndromes
Jan 13, 2011 |
5 / 5 (3) |
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Prion
A prion (pronounced /ˈpriː.ɒn/ ( listen)) is an infectious agent that is composed of protein. To date, all such agents that have been discovered propagate by transmitting a mis-folded protein state; the protein does not itself self-replicate and the process is dependent on the presence of the polypeptide in the host organism. The mis-folded form of the prion protein has been implicated in a number of diseases in a variety of mammals, including bovine spongiform encephalopathy (BSE, also known as "mad cow disease") in cattle and Creutzfeldt-Jakob disease (CJD) in humans. All known prion diseases affect the structure of the brain or other neural tissue, and all are currently untreatable and are always fatal. In general usage, prion refers to the theoretical unit of infection. In scientific notation, PrPC refers to the endogenous form of prion protein (PrP), which is found in a multitude of tissues, while PrPSC refers to the misfolded form of PrP, that is responsible for the formation of amyloid plaques that lead to neurodegeneration.
Prions are hypothesized to infect and propagate by refolding abnormally into a structure which is able to convert normal molecules of the protein into the abnormally structured form. All known prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets. This altered structure is extremely stable and accumulates in infected tissue, causing tissue damage and cell death. This stability means that prions are resistant to denaturation by chemical and physical agents, making disposal and containment of these particles difficult.
Proteins showing prion-type behavior are also found in some fungi and this has been important in helping to understand mammalian prions. However, fungal prions do not appear to cause disease in their hosts and may even confer an evolutionary advantage through a form of protein-based inheritance.
The word prion is a compound word derived from the initial letters of the words proteinaceous and infectious, with -on added by analogy to the word virion.
For more information about Prion, read the full article at
Wikipedia.
This text uses material from Wikipedia and is available under the GNU Free Documentation License.
