To test their findings, the researchers inoculated transgenic mice with prions from sheep
with scrapie, another prion disease causing neurological damage, and determined that these prions have dramatically different biological properties.
This turned out to be a normal protein in the cells of organisms throughout the animal kingdom — but in brains infected
with scrapie and related diseases it turns up in both a normal, soluble form and an abnormal, insoluble form which accumulates in deposits that eventually kill the cells.
Scientists generally assume that BSE arose in cattle whose feed was enriched with a high - protein supplement: sheep parts, unfortunately infected
with scrapie.
But, making assumptions based on past experience
with scrapie, the Southwood committee decided that it was unlikely that BSE could be passed to humans.
Prion specialist Moira Bruce of the Institute for Animal Health's Neuropathogenesis Unit in Edinburgh says that sheep experimentally infected with BSE become ill about as fast as sheep naturally infected
with scrapie.
Moreover, mice infected
with scrapie progressed more quickly to disease.
Not exact matches
The idea is that
scrapie prions might somehow interfere
with the infectivity of BSE prions.
With the scale of the nvCJD threat to public health still unclear, scientists have been busy investigating the relationship between the strains of prions blamed for neurodegenerative illnesses, including the presumed connection between BSE and
scrapie.
Presumably, nucleophilic residues within a
scrapie agent protein undergo carbethoxylation on reaction
with diethyl pyrocarbonate, and subsequent addition of hydroxylamine displaces these carbethoxy groups.
While the origins of BSE remain obscure, one possibility is that the cattle developed the disease by being fed meat and bone meal contaminated
with prions from the sheep
with the disease,
scrapie.