Mad cow

Transmissible spongiform encephalopathies like Creutzfeldt-Jakob disease in humans and bovine TSE, better known as mad cow disease, have certainly caused their share of misery, as well as capturing public attention. A new study appearing in Science, and appearing online at Science Express, describes the work of Ohio State's Jiyan Ma and his colleagues in which they have shown how normal proteins can be converted into prions, the causative agent of spongiform encephalopathies. Prions are abnormally folded proteins which stimulate the formation of other such proteins in the development of the brain disease. However, since the original description of prions in the 1980s it has been unclear how the process operates, with a major drawback being the inability of researchers to employ recombination techniques in the creation of infectious prions. That's exactly what Ma and his associates were able to do. Employing mouse proteins, they determined that it is through an interaction with lipids in the cell membrane that the protein is altered.

They were also able to induce TSE in laboratory mice, which developed TSE symptoms within a few months after recombinant prions were injected into their brains. (On a side note - I'm all for the ethical treatment of animals. I think work like this certainly fits that description). This certainly represents a major step forward in our understanding of prion disease.

Now, for those of you that might have wanted a less dry treatment of mad cow disease - hope this is warped enough for you...