http://www.sciencedaily.com/news/plants_animals/prions/ Learn all about prions and prion disease. How are prions linked to mad cow disease, TSE, Creutzfeldt-Jacob disease and chronic wasting disease? en-us Sat, 17 May 2008 18:05:01 EDT Sat, 17 May 2008 18:05:01 EDT 60 http://www.sciencedaily.com/images/logosmall.gif http://www.sciencedaily.com/news/plants_animals/prions/ For more science articles, visit ScienceDaily. http://www.sciencedaily.com/releases/2008/05/080507105649.htm Prions, the infamous agents behind mad cow disease and its human variation, Creutzfeldt-Jakob disease, also have a helpful side. New research shows that normally functioning prions prevent neurons from working themselves to death. The findings appear in the May 5 issue of the Journal of Cell Biology. Fri, 09 May 2008 05:00:00 EDT http://www.sciencedaily.com/releases/2008/05/080507105649.htm http://www.sciencedaily.com/releases/2008/04/080408144827.htm Amid concern that recipients of certain blood transfusions may risk infection with a deadly protein responsible for the human form of mad cow disease, researchers now report development of a special filter that quickly and effectively removes the protein from blood. Sat, 12 Apr 2008 08:00:00 EDT http://www.sciencedaily.com/releases/2008/04/080408144827.htm http://www.sciencedaily.com/releases/2008/04/080407190603.htm Scrapie can be transmitted to lambs through milk, according to new research. The study provides important information on the transmission of this prion-associated disease and the control of scrapie in affected flocks. Tue, 08 Apr 2008 14:00:00 EDT http://www.sciencedaily.com/releases/2008/04/080407190603.htm http://www.sciencedaily.com/releases/2008/03/080317154402.htm Researchers have identified four separate biochemical subgroups in a selection of cases of Creutzfeldt-Jakob disease. The study suggests that these subgroups could represent distinct prion strains in what is the most common human prion disease. Wed, 19 Mar 2008 08:00:00 EDT http://www.sciencedaily.com/releases/2008/03/080317154402.htm http://www.sciencedaily.com/releases/2008/03/080303093549.htm In an advance in food safety, researchers are reporting development of a nano-sized sensor that detects record low levels of the deadly prion proteins that cause Mad Cow Disease and other so-called prion diseases. The sensor, which detects binding of prion proteins by detecting frequency changes of a micromechanical oscillator, could lead to a reliable blood test for prion diseases in both animals and humans, the researchers say. Wed, 05 Mar 2008 14:00:00 EST http://www.sciencedaily.com/releases/2008/03/080303093549.htm http://www.sciencedaily.com/releases/2007/12/071204154723.htm Scientists have developed two new tests for prions, infectious proteins that cause a number of diseases including "mad cow disease," and a human counterpart, variant Creutzfeldt-Jakob disease. These advances open the door to better understanding and diagnosis of these troubling conditions. Wed, 12 Dec 2007 11:00:00 EST http://www.sciencedaily.com/releases/2007/12/071204154723.htm http://www.sciencedaily.com/releases/2007/11/071130144506.htm Rapid diagnostic testing used to check for the presence of prion diseases such as "mad cow disease" might fail to identify some highly infectious samples, researchers have found. Sat, 01 Dec 2007 20:00:00 EST http://www.sciencedaily.com/releases/2007/11/071130144506.htm http://www.sciencedaily.com/releases/2007/11/071121221704.htm An effective and sensitive new method for detecting and characterizing prions, the infectious compounds behind diseases like mad cow disease, is now being launched. Mad cow disease (BSE), which has caused the death of more than 200,000 cattle and 165 people in the U.K., has now abated. But other prion disorders are on the rise, and there is concern that new strains will infect humans. Thu, 22 Nov 2007 14:00:00 EST http://www.sciencedaily.com/releases/2007/11/071121221704.htm http://www.sciencedaily.com/releases/2007/09/070926192035.htm Lymph nodes can be crucial for spreading low doses of infective prion agents -- the pathogens responsible for conditions such as scrapie and Creutzfeldt-Jakob disease -- into the nervous system, according to new research. Mon, 01 Oct 2007 11:00:00 EDT http://www.sciencedaily.com/releases/2007/09/070926192035.htm http://www.sciencedaily.com/releases/2007/09/070907095625.htm Prion proteins may activate endogenous retroviruses in infected brain cells. Prions – an abbreviation for proteinaceous infectious particles – work as a trigger to a set of diseases of the brain and nervous system, the so-called spongiform encephalopathies. These include BSE in cattle, scrapie in sheep and Creutzfeldt Jakob’s Disease in humans. Prions are structural variants of a normal protein found in healthy tissues – especially in the brain. Sat, 15 Sep 2007 17:00:00 EDT http://www.sciencedaily.com/releases/2007/09/070907095625.htm http://www.sciencedaily.com/releases/2007/09/070905152439.htm Scientists have shown for the first time that small clumps of abnormal prion proteins called oligomers cause the widespread death of neurons. In contrast, much larger prion aggregates known as fibrils proved to be far less toxic. The findings suggest that small protein aggregates play a central role in prion diseases; similar mechanisms have been proposed for the so-called "amyloid" neurodegenerative diseases, including Alzheimer's. The work may provide novel therapeutic approaches for treating people with these conditions. Mon, 10 Sep 2007 23:00:00 EDT http://www.sciencedaily.com/releases/2007/09/070905152439.htm http://www.sciencedaily.com/releases/2007/08/070816121102.htm Scientists have discovered a new protein that may offer fresh insights into brain function in mad cow disease. Fri, 17 Aug 2007 11:00:00 EDT http://www.sciencedaily.com/releases/2007/08/070816121102.htm http://www.sciencedaily.com/releases/2007/07/070705094120.htm Scientists have made significant advances towards the development of a technique that could be used to confirm whether someone is infected with variant Creutzfeldt-Jakob Disease. Tue, 10 Jul 2007 05:00:00 EDT http://www.sciencedaily.com/releases/2007/07/070705094120.htm http://www.sciencedaily.com/releases/2007/07/070706081324.htm The rogue proteins that cause chronic wasting disease (CWD) exhibit a dramatic increase in their infectious nature when bound to common soil particles, according to a new study. Mon, 09 Jul 2007 02:00:00 EDT http://www.sciencedaily.com/releases/2007/07/070706081324.htm http://www.sciencedaily.com/releases/2007/07/070705121847.htm Using baker's yeast and another fungus, researchers report the first successful propagation of a prion from one organism to another. Prions -- infectious, oddly-folded proteins that are the main suspects in fatal neurodegenerative diseases such as Cruetzfeldt-Jakob and bovine spongiform encephalopathy, or "mad cow" -- remain mostly a mystery to scientists. Fri, 06 Jul 2007 17:00:00 EDT http://www.sciencedaily.com/releases/2007/07/070705121847.htm http://www.sciencedaily.com/releases/2007/07/070702145402.htm Sheep infected with scrapie and cows infected with BSE have elevated levels of manganese in their blood before clinical symptoms appear, according to new research. Wed, 04 Jul 2007 20:00:00 EDT http://www.sciencedaily.com/releases/2007/07/070702145402.htm http://www.sciencedaily.com/releases/2007/05/070509161210.htm Prions are highly robust and infectious proteins, most notable for their central role in bovine spongiform encephalopathy, commonly called mad cow disease. But very little is known about how prions form aggregates of malformed proteins that ultimately result in disease. This study provides initial insights into how prions recruit and distort healthy neighboring proteins. Wed, 09 May 2007 23:00:00 EDT http://www.sciencedaily.com/releases/2007/05/070509161210.htm http://www.sciencedaily.com/releases/2007/05/070503135420.htm An oral vaccine can prevent mice from developing a brain disease similar to mad cow disease, according to new research. Prion diseases, which include scrapie, mad cow disease and chronic wasting disease, are fatal, and there is no treatment or cure. Thu, 03 May 2007 20:00:00 EDT http://www.sciencedaily.com/releases/2007/05/070503135420.htm http://www.sciencedaily.com/releases/2007/04/070426162107.htm For the first time, a new study demonstrates that certain rodents can be directly infected with chronic wasting disease and therefore serve as animal models for further study of the disease. Fri, 27 Apr 2007 08:00:00 EDT http://www.sciencedaily.com/releases/2007/04/070426162107.htm http://www.sciencedaily.com/releases/2007/03/070319091103.htm Burying prion-infected carcasses of cattle, deer and other animals in lime may actually enhance the spread of those infectious proteins through soil, a new study suggests. Placing quicklime on carcasses once was thought to be the best way to foster quick decay of bodies and to prevent the spread of disease. Mon, 19 Mar 2007 17:00:00 EDT http://www.sciencedaily.com/releases/2007/03/070319091103.htm http://www.sciencedaily.com/releases/2007/02/070224093334.htm For the first time, experimental results indicate that it is possible to use a resin filter to remove harmful prion proteins from the blood of an infected animal, a finding that has major implications for the removal of infectious prion proteins -- the agents associated with variant Creutzfeldt-Jakob disease, mad cow disease, scrapie and other prion diseases in animals -- during blood transfusions. Mon, 26 Feb 2007 02:00:00 EST http://www.sciencedaily.com/releases/2007/02/070224093334.htm http://www.sciencedaily.com/releases/2007/01/070125114327.htm Do genes affect bovine spongiform encephalopathy--also known as BSE, or "mad cow" disease? Are some cattle more susceptible than others? To address these and other questions, Agricultural Research Service (ARS) scientists at the U.S. Meat Animal Research Center in Clay Center, Neb., have sequenced the bovine prion gene (PRNP) in 192 cattle that represent 16 beef and five dairy breeds common in the United States. Fri, 26 Jan 2007 08:00:00 EST http://www.sciencedaily.com/releases/2007/01/070125114327.htm http://www.sciencedaily.com/releases/2007/01/070123143537.htm Brown University biologists have made another major advance toward understanding the deadly work of prions, the culprits behind fatal brain diseases such as mad cow and their human counterparts. In new work published online in PLoS Biology, researchers show that the protein Hsp104 must be present and active for prions to multiply and cause disease. Wed, 24 Jan 2007 05:00:00 EST http://www.sciencedaily.com/releases/2007/01/070123143537.htm http://www.sciencedaily.com/releases/2007/01/070102140137.htm More accurate genetic tests for diagnosing scrapie disease in sheep have been developed by Agricultural Research Service (ARS) scientists in Clay Center, Neb. They believe this achievement will promote scrapie's eventual eradication. Wed, 03 Jan 2007 14:00:00 EST http://www.sciencedaily.com/releases/2007/01/070102140137.htm http://www.sciencedaily.com/releases/2007/01/070101103354.htm The U.S. Department of Agriculture's Agricultural Research Service have announced initial results of a research project involving prion-free cattle. ARS scientists evaluated cattle that have been genetically modified so they do not produce prions, and determined that there were no observable adverse effects on the animals' health. Mon, 01 Jan 2007 08:00:00 EST http://www.sciencedaily.com/releases/2007/01/070101103354.htm http://www.sciencedaily.com/releases/2006/12/061201180720.htm A new method of treatment can appreciably slow down the progress of the fatal brain disease scrapie in mice. This has been established by German researchers from the Universities of Munich and Bonn together with their colleagues at the Max Planck Institute in Martinsried. They used an effect discovered by the US researchers Craig Mello and Andrew Fire, for which they were awarded this year's Nobel Prize for Medicine. Mon, 04 Dec 2006 14:00:00 EST http://www.sciencedaily.com/releases/2006/12/061201180720.htm http://www.sciencedaily.com/releases/2006/10/061031141414.htm Researchers at the Animal Health Research Centre (CReSA) are developing immunotherapeutical strategies against diseases produced by prion, such as Bovine Spongiform Encephalitis. The most recent results, published in the Journal of Virology, show that important advances have been made in tests using DNA vaccines on animal models, enabling a significant delay in the arrival of symptoms. In the long term, this research could lead to the production of treatment for humans. Wed, 01 Nov 2006 11:00:00 EST http://www.sciencedaily.com/releases/2006/10/061031141414.htm http://www.sciencedaily.com/releases/2006/10/061030120759.htm The urgent search for a medication to treat prion diseases has led scientists in Germany to synthesize a new group of compounds, including one that is 15 times more potent than an approved drug now being tested in clinical trials. Their report is scheduled for the Nov. 2 issue of the biweekly ACS Journal of Medicinal Chemistry. Tue, 31 Oct 2006 14:00:00 EST http://www.sciencedaily.com/releases/2006/10/061030120759.htm http://www.sciencedaily.com/releases/2006/08/060820195413.htm A study published today in the online edition of the Journal of the Royal Society Interface has been exploring the likelihood that vCJD might be spread via the reuse of surgical instruments, and calls for more data in order to allay fears over the possible transmission of vCJD. Mon, 21 Aug 2006 08:00:00 EDT http://www.sciencedaily.com/releases/2006/08/060820195413.htm http://www.sciencedaily.com/releases/2006/07/060707151953.htm A team of researchers at The Scripps Research Institute, the University of California, San Diego (UCSD), and Rocky Mountain Laboratories of the National Institute of Allergy and Infectious Diseases of the National Institutes of Health (NIH), has shown for the first time that laboratory mice infected with the agent of scrapie -- a brain-wasting disease of sheep-demonstrate high levels of the scrapie agent in their heart 300 days after being infected in the brain. Fri, 07 Jul 2006 05:00:00 EDT http://www.sciencedaily.com/releases/2006/07/060707151953.htm http://www.sciencedaily.com/releases/2006/07/060707021040.htm In the July 7, 2006, issue of the journal Science, researchers at the University of Texas Medical Branch at Galveston (UTMB) describe experiments that may soon lead to a test that will enable medical science to estimate how many people are infected with the human form of mad cow disease, which can take as long as 40 years before manifesting itself. Thu, 06 Jul 2006 11:00:00 EDT http://www.sciencedaily.com/releases/2006/07/060707021040.htm http://www.sciencedaily.com/releases/2006/06/060629105141.htm Brittleness is often seen as a sign of fragility. But in the case of infectious proteins called prions, brittleness makes for a tougher, more menacing pathogen. Howard Hughes Medical Institute researcher have discovered that brittle prion particles break more readily into new "seeds," which spread infection much more quickly. Thu, 29 Jun 2006 05:00:00 EDT http://www.sciencedaily.com/releases/2006/06/060629105141.htm http://www.sciencedaily.com/releases/2006/04/060428141132.htm Researchers have demonstrated spread of senile amyloidosis from affected mice to their nursing offspring. The paper by Korenaga et al., "Transmission of amyloidosis in offspring of mice with AApoAII amyloidosis," appears in the March issue of the American Journal of Pathology and is highlighted on the cover of the Journal. Fri, 28 Apr 2006 08:00:00 EDT http://www.sciencedaily.com/releases/2006/04/060428141132.htm http://www.sciencedaily.com/releases/2006/04/060414013751.htm Scientists have confirmed that prions, the mysterious proteins thought to cause chronic wasting disease (CWD) in deer, latch on tightly to certain minerals in soil and remain infectious. Fri, 14 Apr 2006 05:00:00 EDT http://www.sciencedaily.com/releases/2006/04/060414013751.htm http://www.sciencedaily.com/releases/2006/03/060331010409.htm While newly published research confirms that under laboratory circumstances prion-protein can be absorbed across the gut, it also shows that this is unlikely to occur in real life. In addition, the results show that the places in the gut that do take up these disease-associated proteins are different from the locations where infectivity is known to be amplified. The findings will be published in the Journal of Pathology. Fri, 31 Mar 2006 02:00:00 EST http://www.sciencedaily.com/releases/2006/03/060331010409.htm http://www.sciencedaily.com/releases/2005/11/051122183641.htm Researchers at Binghamton University have a first-ever opportunity to determine if Chronic Wasting Disease (CWD) in deer can be spread to humans who ingest "infected" meat. Tue, 22 Nov 2005 08:00:00 EST http://www.sciencedaily.com/releases/2005/11/051122183641.htm http://www.sciencedaily.com/releases/2005/10/051022111510.htm Research at Yale University School of Medicine shows that infection with a weak strain of Creutzfeldt-Jacob Disease (CJD) prevents infection by more virulent strains and that the protection requires persistent replication by the infectious agent, but not misfolded prions. Protection with a weak animal agent may account for the low incidence of CJD linked to Mad Cow Disease in people. Sat, 22 Oct 2005 05:00:00 EDT http://www.sciencedaily.com/releases/2005/10/051022111510.htm http://www.sciencedaily.com/releases/2005/10/051020091336.htm The scientific magazine <i>Brain Research</i> has recently published the results of research work by scientists from the University of Navarra. The work describes the presence and location of the cellular prion protein (PrPC) in the brain of the rat and characterises the neurones expressed therein, above all within the cerebral cortex of this rodent. Thu, 20 Oct 2005 11:00:00 EDT http://www.sciencedaily.com/releases/2005/10/051020091336.htm http://www.sciencedaily.com/releases/2005/08/050829080815.htm Researchers have found a way to detect in blood the malformed proteins that cause "mad cow disease," the first time such "prions" have been detected biochemically in blood. The discovery is expected to lead to a much more effective detection method for the infectious proteins responsible for brain-destroying disorders, such as bovine spongiform encephalopathy (BSE) in cattle and variant Creutzfeldt-Jakob disease (vCJD) in humans. Mon, 29 Aug 2005 08:00:00 EDT http://www.sciencedaily.com/releases/2005/08/050829080815.htm http://www.sciencedaily.com/releases/2005/06/050615001037.htm Abnormal prion proteins are little understood disease agents involved in causing horrific brain-wasting diseases such as Creutzfeldt-Jacob disease in people, mad cow disease in cattle and chronic wasting disease in deer and elk. Now, new research suggests that a variant form of abnormal prion protein--one lacking an 'anchor' into the cell membrane--may be unable to signal cells to start the lethal disease process. Wed, 15 Jun 2005 05:00:00 EDT http://www.sciencedaily.com/releases/2005/06/050615001037.htm http://www.sciencedaily.com/releases/2005/05/050524225513.htm Scientists for the first time have watched agents of brain-wasting diseases, called transmissible spongiform encephalopathies (TSE), as they invade a nerve cell and then travel along wire-like circuits to points of contact with other cells. These findings will help scientists better understand TSE diseases and may lead to ways to prevent or minimize their effects. TSE, or prion, diseases include scrapie in sheep and goats; chronic wasting disease in deer and elk; mad cow disease in cattle; and Creutzfeldt-Jacob disease in humans. Wed, 25 May 2005 02:00:00 EDT http://www.sciencedaily.com/releases/2005/05/050524225513.htm http://www.sciencedaily.com/releases/2005/05/050514111648.htm NYU School of Medicine scientists have created the first active vaccine that can significantly delay and possibly prevent the onset of a disease in mice that is similar to mad cow disease. Sat, 14 May 2005 08:00:00 EDT http://www.sciencedaily.com/releases/2005/05/050514111648.htm http://www.sciencedaily.com/releases/2005/04/050424200507.htm Although prions from one species rarely infect other species, researchers suspected that the species barrier is overcome when prions in the two species share a certain level of genetic sequence similarity. Now, new research in mammals and yeast show that when prions do cross the species barrier, it may be because protein fibrils formed by the prions share the same distinctive shape in both species. Mon, 25 Apr 2005 02:00:00 EDT http://www.sciencedaily.com/releases/2005/04/050424200507.htm http://www.sciencedaily.com/releases/2005/02/050205105557.htm Prions, infectious proteins associated with bovine spongiform encephalopathy (BSE) or Mad Cow Disease, were previously thought to accumulate mainly in the brain, but Yale and University of Zurich researchers report in Science that other organs can also become infected. Tue, 08 Feb 2005 02:00:00 EST http://www.sciencedaily.com/releases/2005/02/050205105557.htm http://www.sciencedaily.com/releases/2004/07/040730092224.htm Scientists have produced a prion protein that can trigger the development of a neurological disorder in mice that is similar to "mad cow" disease, according to a new study supported by the National Institute on Aging. Fri, 30 Jul 2004 00:00:00 EDT http://www.sciencedaily.com/releases/2004/07/040730092224.htm http://www.sciencedaily.com/releases/2004/05/040526064629.htm With funding from the U.S. Environmental Protection Agency, a group of UW-Madison researchers will investigate what happens if infectious prion proteins - considered the cause of chronic wasting disease and mad cow disease - enter wastewater treatment plants. Thu, 27 May 2004 00:00:00 EDT http://www.sciencedaily.com/releases/2004/05/040526064629.htm http://www.sciencedaily.com/releases/2004/04/040409092722.htm Researchers at Case Western Reserve University School of Medicine have taken a major step towards understanding how abnormal prion proteins, the suspected cause of mad cow and related diseases, change shape to jump from one animal species to another. Fri, 09 Apr 2004 00:00:00 EDT http://www.sciencedaily.com/releases/2004/04/040409092722.htm http://www.sciencedaily.com/releases/2004/03/040323070139.htm Researchers have identified the amino acid sequences that allow prions to aggregate and replicate - and thereby pass through generations of cells - and prove this by designing an artificial yeast prion that does not exist in nature. Tue, 23 Mar 2004 00:00:00 EST http://www.sciencedaily.com/releases/2004/03/040323070139.htm