Those Insidious Prions
I may work in an Immunology Lab, but when you spend your days on the paperwork, you don’t learn a terrible amount about the – you know – science. This is why I seek out anything lay-friendly I can get my hands on. Lately, I’ve been collecting notes on some of the most basic elements of immunology; in this case, it’s been all about blood.
In advance of my attempt to explain it to non-scientists, I offer a quickie introduction to the dreaded Prion. Why is it dreaded?
A prion is a misshapen protein that acts like an infectious agent (hence the name, which comes from the words protein and infection).
Prions cause a number of fatal diseases such as mad cow disease in cattle, scrapie in sheep and kuru and Creutzfeldt-Jakob disease (CJD) in humans. There is no cure and potential treatments are highly speculative.
In recent years, however, biologists have discovered several animals that are immune to prion diseases. These include horses, dogs and rabbits. Nobody knows why.
That’s from a recent piece in MIT’s Technology Review.
Basically, proteins fold themselves. Sometimes, they fold themselves poorly, like when I get fancy with paper-airplanes. When this happens, they can become prions, and those things are bad news. A creature infected with such a disease experiences nervous system degeneration.
The University of Ballarat’s Jiapu Zhang thinks he’s on to something:
Zhang has simulated how these proteins change shape as their temperature and pH changes.
His conclusion is that the immune proteins are more stable than the others because of a salt bridge that connects two parts of the immune proteins “like a taught bow string”. This prevents them from misfolding into an infectious form.
So salt could be the answer? All I can say is follow the data. I’d love to learn that someone has duplicated his findings. All kinds of potential problems with our nervous system could be addressed. So, there.









