To better understand for what reas...

To better understand for what reason transmissible spongiform encephalopathies (TSEs), as it was as scrapie and mad abash disease, "jump" and adapt to recent species, researchers at the National Institute of Allergy and Infectious Diseases have examined the proces from which scrapie transfers from hamsters to mice. According to an Oct 17 2001 of recent origins release from the institute, researchers first inoculated mice with a strain of hamster scrapie, and then closely monitored the mice for several years. This assign places to of mice never became sick, yet scientists found that the scrapie agent may have persisted in these mice at of the same heights too low for standard trials to detect.

Researchers fix that although the mice did not carry enough of the scrapie agent to be lay opened on tests, they did carry enough to reinfect hamsters, who were injected with brain extracts from the infected mice. Although these ensues do not necessarily apply to other TSE and other species, researchers hint that TSEs may be more widespread than originally believed. As a come researchers call for more sensitive diagnostic ordeals and more vigilance in monitoring the spread of TSEs

The reflection also found that, under the right conditions, scrapie gradually adapted to cause illness in mice during a one- to two-year period. In the original cluster of infected mice, the scrapie agent at no time caused illness; however, when the agent was transferred from these mice to other arranges of mice, the disease grew stronger making the newly infected assign places to of mice sick, according to the release. Researchers indicate that the scrapie agent replicated faster in additional clumps of mice and became more lethal across time. Researchers also noted that scrapie adapted in the mice in different ways. Incubation periods varied widely, and the disease affected different parts of the mice's brains.

Also known as prion diseases, TSE include chronic wasting disease in deer and moose and Creutzfeldt-Jakob Disease in humans. The hallmark of TSE is misshapen protein atoms that clump together and accumulate in brain tissue. These abnormal prion proteins are the likely cause of the brain damage that fall outs with TSE diseases. According to the release, scientists believe the misshapen prion proteins in some way induce normal prion proteins to form incorrectly and that these abnormal atoms may spread the disease to other individuals.

thought Examines How Prion Disease Adapts to fresh Species (news release, Washington, DC: National Institutes of Health, National Institute of Allergy and Infectious Disease, Oct 17 2001) http://www.nih.gov (accessed 18 Oct 2001)

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