BSE is a fatal neurodegenerative brain disease in cattle. Cattle can contract BSE by eating feed made from bovine tissues that are contaminated, a practice that is banned in many world regions. The cause of BSE is unknown, butit is believed to be a prion disease (a prion is a self-replicating protein) or a virus that possesses nucleic acids carrying genetic information. The disease affects the brain and spinal cord of cattle, and lesions in these tissues look “spongy.” BSE is a Transmissible Spongiform Encephalopathies (TSE) and similar diseases can infect animals and humans.

Canada- New case of mad cow disease, industry says beef trade not affected
04 March 2011
Am770chqr.com [edited] [BITES]
Canada is dealing with a new case of mad cow disease. The dairy cow discovered brings to 18 the number of cattle that have been found with the fatal brain disease in Canada since 2003. The Canadian Food Inspection Agency confirmed the case in the six-year-old cow last month. Canada is categorized as being a controlled risk for bovine spongiform encephalopathy. The cow did not enter the food chain for people or animals and the new case should not hurt Canada's global beef trade status.

Eyes of cattle may detect mad cow disease
08 September 2010
American Chemical Society [edited] [BITES]
Scientists are reporting evidence that a peek into the eyes of cattle may become the basis for a long-sought test to detect infection with the agent that causes Mad Cow Disease. A study has recently been publish about observing the tell-tale glow given off by eyes infected with the Mad Cow agent. Past studies suggest that chemical changes in an animal's retina, the light sensitive nerve tissue in the back of the eye, may provide a basis for detecting prion diseases. Scientists suggest that eye tests based on the findings could become important in the future for fast, inexpensive diagnosis of prion diseases, and other neurological diseases.

What drove the cow mad? Lessons from a tiny fish
09 Mar 2009
Public Library of Science - Sally Hubbard [iFSN]
Regulation of embryonic cell adhesion by the prion protein
For over twenty years, scientists have known that a normal protein in the brain, PrP, or prion protein, can turn harmful and cause deadly illnesses like Creutzfeldt-Jakob disease (CJD) in humans, and bovine spongiform encephalopathy (BSE) in cattle. What they could not explain is why large amounts of this normal protein are produced by our bodies in the first place. In a new study published in this week's PLoS Biology, researchers from the University of Konstanz in Germany reveal that PrP indeed plays a beneficial role for the organism – PrP helps cells communicate with one another during embryonic development.
In prion diseases, what transforms the normal PrP protein into a life-threatening substance is the abnormal alteration of its chemical structure. Moreover, prions have the treacherous ability to replicate by imprinting their abnormal structure into healthy PrPs, thereby generating new pathogenic particles. While this "conversion" process explains how prions are disseminated, "An abnormal function of the prion protein is considered to be one of the reasons for neuronal degeneration," explains Dr. Edward Málaga-Trillo, leader of the study in Konstanz. However, the normal function of PrP has remained an unsolved mystery for many years. Until now, all previous experiments in genetically modified mice had failed to provide conclusive evidence, as these animals lacking PrP seemed perfectly healthy.
The scientists from Konstanz were able to show that the lack of PrP can cause clear physiological abnormalities in a living animal and the trick was to use the tiny zebrafish as a model.
When the researchers from Konstanz microinjected zebrafish eggs with morpholinos, DNA-like molecules that prevent the normal production of PrP, the treated zebrafish embryos were unable to develop normally and eventually died. The proteins in the fish embryos normally found at cell-to-cell contact sites disappeared, rendering these cells unable to communicate and carry out the differentiation program that shapes the major structures of the body, including the nervous system.
"We were then able to prove that PrP serves as a glue element, bringing cells together and keeping them in contact," explains co-author Dr. Gonzalo Solis, member of the team at the laboratory of Prof. Claudia Stürmer. "When two neighboring cells make contact, they become able to exchange important signals that affect the function of a tissue in the body."
Although the work by Málaga-Trillo, Solis, and colleagues does not offer an immediate cure for CJD or BSE, the team from Konstanz has fit together the first pieces of a complex puzzle, which may widen our understanding of prion diseases and provide hope for their effective treatment.

United Kingdom - Antibody key to treating variant CJD, scientists find
04 Mar 2009
University of Liverpool - Samantha Martin [edited][iFSN]
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.
Variant Creutzfeldt-Jakob Disease (vCJD) is part of a family of rare progressive neurodegenerative disorders, called prion diseases, which affect both animals and humans. It is thought that those who have developed vCJD became infected through the consumption of cattle products contaminated with Bovine Spongiform Encephalopathy (BSE) – a brain disorder in cows, commonly known as Mad Cow Disease.
Prion diseases can develop when a naturally occurring brain prion protein called, PrP, comes into contact with infectious prions. This converts PrP into a form that has a different shape, and eventually leads to a build-up of protein in the brain, causing brain cells to die. It is thought that immunisation with antibodies that can 'stick' to PrP could treat and even prevent the development of the disease.
To understand the 'connection' between the antibody and the protein, scientists at Liverpool used X-ray crystallography technology to build a three-dimensional picture of the binding between an antibody called ICSM18 – designed to 'stick' effectively to prion proteins – and PrP cells.
Samar Hasnain, Professor of Molecular Biophysics at the University, explains: "To pin-point where the antibody 'sticks' to the protein we used X-ray crystallography, pioneered by Nobel Prize winner Max Perutz. Significantly we found that the point at which the protein and antibody came together was also where scientists at the Medical Research Council (MRC) Prion Unit had identified a single amino acid, which we now know has a significant impact on a patient's susceptibility to prion disease."
Scientists at the MRC Prion Unit, University College London, who collaborated on the research, have found that ICSM18 could help prevent brain cells from becoming infected as well as reverse early damage caused by the disease.
Professor John Collinge, Director of the MRC Prion Unit, added: "We have shown that ICSM18 has the highest therapeutic potential in animal and cell based studies, but we have yet to establish its impact on people who have vCJD or other prion diseases. We are currently working, however, to make human versions of the antibodies for future trials in people."

Netherlands - 3rd vCJD death
2 Feb 2009
AFP/Expatica [edited Promed] The 3rd person in the Netherlands died of the human variant of mad cow disease, Creutzfeldt-Jakob (vCJD), at the beginning of January 2009. The 3rd person in 4 years has died from the human form of mad cow disease in the Netherlands, the national health research agency RIVM said on Monday [2 Feb 2009].
"The patient died at the beginning of January [2009]," it announced in a press statement. "An investigation has confirmed that the patient died of the variant form of Creutzfeldt-Jakob disease." The RIVM did not say how, when or where the patient contracted the disease but pointed out that the incubation period, from infection to the display of symptoms, could last decades. Investigations were ongoing into the "very rare chance" that the patient may have infected other people. The statement stressed that Dutch beef was safe, explaining that all slaughtered cows are tested for BSE since 2001.
The RIVM said 2 other people have died of the disease in the Netherlands, one diagnosed in 2005 and the other in 2006. "About 200 people have died of the disease in the world, 167 of them in Britain," said the statement.

France - Institut de Veille Sanitaire - as of 30 Jan 2009
30 Jan 2009
IVS - Maladie de Creutzfeldt-Jakob et maladies apparentees [French, trans. & summ. Mod.CP, edited] [Promed] During the period 1992 to 2008, there were 23 cases of vCJD, all now deceased. They occurred between 1996 and 2007: One case in 1996, one in 2000, one in 2001, 3 in 2002, none in 2003, 2 in 2004, 6 in 2005, 6 in 2006, 3 in 2007, and none so far in 2008. There were 12 male and 11 female patients.
Their ages at time of death ranged from 19 to 58 years (mean 39); 6 of the patients resided in the Ile-de-France [Paris area] and 17 in the provinces. All the cases were met-met homozygotes for codon 129 of the prion protein gene. No special risk factors were evident, which distinguished these patients from those with other forms of CJD (sporadic, genetic, iatrogenic). However, one patient had visited the UK at regular intervals. Totals for all types of CJD cases in the year 2008
As of 30 Dec 2008 in France, during the course of 2008, there have been 1438 referrals, 76 deaths from sporadic CJD, 3 deaths from iatrogenic CJD, 8 from familial CJD, none from GSS, and none from vCJD. As of 30 Jan 2009, 106 cases were referred with no CJD diagnoses recorded.

Prion protein function
21 Dec 2008
BBC News online [edited] [Promed]
It is reported that the brain protein which has a hand, when defective, in the lethal disease CJD may also be involved in aiding our sense of smell. Mice bred to lack the prion protein could not find buried food or choose between smells. Columbia University scientists said some symptoms of prion disease might be due to the loss of the protein's original role. The study was published in the journal Nature Neuroscience.

Is there more to prion protein than mad cow disease?
29 Sep 2008
BioMed Central - Charlotte Webber [edited][iFSN]
Prion protein, a form of protein that triggers BSE, is associated with other brain diseases in cattle, raising the possibility of a significant increase in the range of prion disease. Publishing their findings in the open access journal BMC Veterinary Research, scientists have detected changes in the production and accumulation of the prion protein in the brains of cattle with a rare neurodegenerative disorder.
Martin Jeffrey of the Veterinary Laboratories Agency led a research team that tested 15 brains of cattle with idiopathic brainstem neuronal chromatolysis and hippocampal sclerosis (IBNC). They are the first group to show that the brains of animals with this disease accumulate prion protein (PrP), the protein that misfolds to cause BSE and which, when transmitted to humans through the food chain, can cause the deadly Variant Creutzfeldt-Jakob disease. IBNC is a rare neurological disease of adult cattle. It was first characterised in 1988 following laboratory tests from cattle suspected of having BSE. Although IBNC has some clinical similarities to BSE, the brains of affected cattle do not have the neuronal vacuolation (lesions) typical of BSE. Further laboratory tests suggest that the misfolded form of PrP, which accumulates in the brains of BSE cases, is not present in IBNC cases. Commercial BSE testing kits did not detect the telltale, BSE-inducing form of PrP either. However, the presence of increased levels of PrP was detected. "We've shown for the first time that prion protein is somehow involved in IBNC," says Jeffrey, "In this disease, there is an association with abnormally high levels of a prion protein in the brain but clearly this PrP is in a different form to that involved in BSE and CJD. This may have implications for diagnosis and recognition of typical forms of BSE as well as the related diseases in sheep, deer and in man.

'Novel' CJD
9 Jul 2008
BBC News online [edited] [Promed]
'New CJD type' discovered in US
A new form of Creutzfeldt-Jakob disease (CJD) may have been uncovered in a handful of patients in the US. So far, 10 people have died from a fast-advancing form of fatal dementia called PSPr, according to a report in New Scientist [see (4) below]. Patients develop the trademark brain damage associated with CJD -- the type not linked to BSE -- but scientists believe there may be a genetic cause [familial CJD].
Experts in the UK are now checking records to see if any cases have happened across the Atlantic. There are between 50 and 100 new cases of so-called sporadic CJD diagnosed in the UK every year. Unlike "variant CJD," the human form of BSE in cows contracted by eating contaminated brain tissue in the 1980s and 1990s, the cause of most cases of sporadic CJD is unknown.
The new cases were referred to CJD surveillance units in the US because they were a suspiciously fast-advancing form of dementia with additional symptoms such as the loss of the ability to speak and move, even though traditional tests that normally help diagnose CJD proved negative. Post-mortems on those who died revealed the familiar "spongy" brain tissue, covered with tiny holes. These are thought to be caused by the accumulation of "prions," a misshapen version of a normal brain protein.
Dr. Pierluigi Gambetti, director of the US National Prion Disease Pathology Surveillance Center, in Ohio, said that he believed the newly discovered type had probably "been around for years, unnoticed." He suggested one interesting common factor was that the patients came from families with a history of dementia, suggesting a genetic cause, but did not carry the gene traditionally associated with a small number of sporadic CJD cases.
Dr. Mark Head, from the UK's National CJD Surveillance Unit, in Edinburgh, said the finding had prompted scientists to start reviewing cases of sporadic CJD in this country to see if there were any of the newly discovered version. He said: "What is interesting about this is that it may mean there are other genes out there waiting to be found which are associated with prion disease, and looking at these patients in the US could help find them.
Related stories
9 Jul 2008 - New CJD-like disease kills 10 people
New Scientist [edited] pd
A new form of fatal dementia has been discovered in 16 Americans, 10 of whom have already died of the condition. It resembles Creutzfeldt-Jakob disease -- with patients gradually losing their ability to think, speak and move -- but has features that make it distinct from known forms of CJD. No one yet knows how the disease originates, or under what conditions it might spread. Nor is it clear how many people have the condition. Since Gambetti's team wrote a paper describing an initial 11 cases referred to his centre between 2002 and 2006 (Annals of Neurology, vol 63, p 697), another 5 have come to light. "So it is possible that it could be just the tip of the iceberg," Gambetti says.

South Korea - Gyeonggi to end consumption of downer cows
08 Jul 2008
Chosunilbo [edited] [iFSN]
According to this story, about 600 so-called downer cattle have been slaughtered and sold for consumption in Gyeonggi Province every year. The affliction, which causes animals to stagger, has nothing to do with mad cow disease, but the Gyeonggi provincial government decided no longer to slaughter such cattle in the future but buy all of them to dispose of for purposes other than eating. Amid massive protests against U.S. beef imports and public confusion over the distinction between downer cows and animals infected with BSE, the province will increase the number of cattle subject to inspection for mad cow disease to 5,040 animals annually, and buy all downer cattle to process them as industrial oil and fat through high-temperature sterilizing treatment, instead of selling them as beef.

United Kingdom - National CJD Surveillance Unit -- Monthly statistics & 2007 totals
07 Jan 2008
UK National CJD Surveillance Unit, monthly statistics, 2007 [edited] Monthly Creutzfeldt-Jakob disease statistics -- as of 7 Jan 2008
These following figures show the number of suspect cases of CJD referred to the CJD surveillance unit in Edinburgh and the number of deaths of definite and probable variant Creutzfeldt-Jakob disease [abbreviated in ProMED-mail as CJD (new var.) or vCJD], the form of the disease thought to be linked to BSE (bovine spongiform encephalopathy). Definite and probable vCJD cases in the UK as of 7 Jan 2008 Summary of vCJD cases – deaths Deaths from definite vCJD (confirmed): 114 Deaths from probable vCJD (without neuropathological confirmation): 48 Deaths from probable vCJD (neuropathological confirmation pending): 1 Number of deaths from definite or probable vCJD (as above): 163 Summary of vCJD cases – alive Number of probable vCJD cases still alive: 3 Total Number of definite or probable vCJD (dead and alive): 166 These data indicate that there have been no new cases diagnosed during the past month, but the number of patients alive has decreased by one. These data are still consistent with the view that the vCJD outbreak in the UK is in decline (although the incidence curve may be developing a tail). The peak number of deaths was 28 in the year 2000, followed by 20 in 2001, 17 in 2002, 18 in 2003, 9 in 2004, 5 in 2005, 5 in 2006, and 5 in 2007. Totals for all types of CJD cases in the year 2007 As of 31 Dec 2007 in the UK in the year 2007, there were 111 referrals, 47 deaths from sporadic CJD, 2 deaths from iatrogenic CJD, 4 deaths from familial CJD, one from GSS, and 5 deaths from vCJD.


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