According to BBC News, coroners in England and Wales are reluctant to carry out tests for vCJD because it is outside their scope of their job and might undermine their neutrality, despite pleas from scientists and the government that this might be the only effective way to determine how many people might be infected. Professor John Collinge, a member of the government appointed Spongiform Encepalopathy Advisory Committee (SEAC), told the BBC that he hoped the coroners would be able to do the tests because he couldn't see "any other way for us to get this information at the moment". vCJD is short for variant Creutzfeldt-Jakob disease, a brain-wasting disease that humans get from eating beef from cattle infected with Bovine Spongiform Encephalopathy (BSE). There is also an unknown risk of cross infection from blood transfusions and surgery.
A new study shows that nervous system integrity and axonal properties may play a key role in prion diseases. The findings, from researchers at the Rudolf Virchow Center and the Institute of Virology of the University of WÃ rzburg, expand our understanding of the development of prion disease and suggest novel targets for therapeutic and diagnostic approaches in its early stages. Details are published August 21 in the open-access journal PLoS Pathogens. Despite growing awareness of prion diseases, such as bovine spongiform encephalopathy (BSE) and the human variant, Creutzfeldt-Jakob disease, the molecular mechanisms responsible for their development are still not completely understood. These diseases are associated with neuropathological symptoms that include dementia, motor system defects and amnesia, although previous observations identified molecular hallmarks in the absence of these neuropathological symptoms, creating a paradox.
For the first time, Whitehead Institute researchers have shown definitively that mutations associated with prion diseases are sufficient to cause a transmissible neurodegenerative disease. The discovery is reported in the August 27 edition of the journal Neuron. Until now, two theories about the role mutations play in prion diseases have been at odds. According to one theory, mutations make carriers more susceptible to prions in the environment. Alternatively, mutations themselves might cause the disease and the spontaneous generation of transmissible prions. Prions cause several diseases, including Creutzfeldt-Jakob disease (CJD) in humans, bovine spongiform encephalitis (BSE, or "mad cow disease") in cows, and scrapie in sheep. Some prion diseases, like BSE, can be transmitted from feed animals to humans.
A collaboration between scientists at Vanderbilt University and the University of California, San Francisco has led to the first direct information about the molecular structure of prions. In addition, the study has revealed surprisingly large structural differences between natural prions and the closest synthetic analogs that scientists have created in the lab. Prions are the infectious proteins responsible for human Creutzfeldt-Jakob disease, bovine spongiform encephalopathy, or "mad cow" disease, scrapie in sheep and several other related nervous system disorders in mammals. For a number of years, scientists have been using the tools of genetic engineering to create synthetic versions of these particles so they could study them more easily. Although researchers have made particles that appear identical to natural prions, they have had trouble duplicating their infectious behavior.
Specific cells within the immune system could help explain why younger people are more susceptible to variant CJD, scientists believe. Patients diagnosed with variant CJD are, on average, 28 years old but it has been unclear why older people are not as affected by the disease. Research at The Roslin Institute of the University of Edinburgh has identified specific cells within the immune system that attract corrupted proteins - known as prions - linked to variant CJD and encourage them to multiply and spread. The study, published in the Journal of Immunology, looked at how these cells behaved in mice and found that the cells were impaired in older mice. As a result, they were unable to trap and replicate the prions and the mice did not develop clinical disease. Neil Mabbott, of The Roslin Institute, said: "It has always been unclear why younger people were more susceptible to variant CJD and the assumption that they were more likely to eat cheap meat products is far too simplistic.