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The best science had it that the prion agent of the disease couldn't jump the species barrier.
There also is evidence that the prion can persist in soil and infect healthy animals that ingest contaminated soil particles.
Dr. Bruce Chesebro, chief of the Laboratory of Persistent Viral Diseases at the federal Rocky Mountain Laboratories, said the experiment showed that the prion produced something in the mice.
But recent research shows that the prion, like other misfolding proteins, early on forms tiny toxic fibrils, or pores, that can literally poke holes in cells, a finding that may account for the spongy cavities seen in victims' brains.
It has become evident that the prion protein (PrP) can form a diverse range of self-replicating structures in addition to bona fide PrPSc or strain-specific PrPSc variants.
It is now well established that the prion protein (PrP) has an influence on cellular copper metabolism.
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Once that happens, the prion form takes over rapidly.
The underlying molecular process that causes the prion protein to form in these cases is unknown.
Genetic polymorphisms that alter the prion protein in humans and sheep are associated with transmissible spongiform encephalopathy susceptibility or resistance.
Once they start accumulating, the theory is that the prions form a runaway chain reaction that ultimately destroys brain tissue.
There is a small chance that the prions discovered in the appendix tissues are unrelated to the flood of BSE-infected meat that entered the food chain in the 1980s and 1990s.
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