http://www.physorg.com/news6069.html

Without reading the entire report on their methods, I"d be skeptical about this report. The reason blood tests haven"t been used is because the concentration of the prion protein is too low in blood. Somehow they are "distilling" the blood or something along those lines to increase the level of prions in the the blood sample to a detectable level. I"d want to know how this is done, and whether they really are prions or a very similar protein that isn"t harmful like bse.

i haven't not read the scientific article yet, but prions are malformed proteins that are capable of converting normal proteins of the same sequence into malformed ones. i assume that the sonication of the protein solution exacerbates this process and creates more malformed proteins to a concentration that can be assayed. that is, if there were no malformed proteins (no vCJD) then that sonication would not create more prions.

Geekbruin, the bottom line is probably that nobody has proved rigorously just what the repeated sonication steps contribute to the amplification process, but the rationale for trying sonication in the first place would be that the prion form of the protein clumps together. In order to increase the surface area at which these clumps might interact with the normally folded protein, you would want to break break them up, ideally converting them to a monomeric (but still malfolded) form.

It will be extremely interesting to see whether this method can detect malfolded prion protein in the very early asymptomatic stages of the disease. In theory, it might. This would require blood levels of the malfolded monomer to remain rather constant over time while the levels in the brain continue to increase. This might be the case, but then again, it might not.