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Artificial Prion Created

jabberjaw writes "Nature is reporting that researchers at the University of California San Diego have created a synthetic prion which, when injected into mice will bring about symptoms similar to those displayed by cattle suffering from bovine spongiform encephalopathy, aka mad cow disease. The researchers first crafted healthy prion proteins using bacteria. They then shook these proteins until they resembled the tangled structure of an unhealthy prion. Afterwords, these prions were injected into the brains of mice who fell ill two years later. Perhaps someone who is more familiar with this field of research would care to fill us in on the details as the article was rather light."

12 of 496 comments (clear)

  1. whoo hoo? by grasshoppa · · Score: 5, Funny

    We gave mice mad cow disease! Yay!

    This is the first step, I'm sure, to giving it to politicians.

    On perhaps a bit more serious of a note, what does this do for us? Is this highlighting that we now know HOW the disease is created, so we can start developing a cure? Or am I wrong. Again. :)

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    1. Re:whoo hoo? by MadBiologist · · Score: 5, Insightful

      That's most likely... by creating a model disease in a biological system, different drugs can be tried out on it to test efficacy.

      There are all sorts of protocols like this already... ie, EAE (Experimental Allergic EncephaloMyelitis) where they give mice... um... artificial MS, then test drug canidates out on them to see what the effect is. It's not very nice to watch.

      That's why I'm glad that I'm in molecular studies. However, it's done to help people with these diseases, and animal reseach is really the only way to conduct some of these tests.

      Peace...

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    2. Re:whoo hoo? by mrfunnypants · · Score: 5, Informative
      This is huge because it was still not very clear that Prions even existed. Many people in the field didn't agree with the very existence and this group has basically just proven that in fact proteins can cause disease. In the world if you had started sprouting off that proteins caused disease in as late as the 80's scientist would laugh and remove you from any future funding. Just to give you an idea, read this link at UCSD where Prions are discussed:

      ucsd link

      As for your question of how the disease works. Theories were made about how this was possible, dealing with stereochemistry of the prion proteins causing your natural protein to switch its stereochemistry to the unnatural state found within the Prions in a cascade effect resulting in death. It appears this group may have verified this theory.

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    3. Re:whoo hoo? by bcrowell · · Score: 5, Funny

      We gave mice mad cow disease! Yay!
      The lesson is clear. If someone comes at you with a big long needle, and wants to stick it in your brain, don't let him!

    4. Re:whoo hoo? by BrokenHalo · · Score: 5, Informative
      Am I way off base here?

      Yes.

      Prion diseases (to oversimplify a bit) are caused by incorrectly folded proteins that induce "correctly" folded proteins to assume the prion form. They are typically communicated by ingestion of meat (or meat products) from infected animals.

      Bubonic plague is a bacterial infection by Yersinia pestis.

  2. the bottom line by Anonymous Coward · · Score: 5, Funny

    Don't eat the beef that comes from those experimental mice.

  3. two years?? by Anonymous Coward · · Score: 5, Funny

    they should get an award just for keeping mice alive for two years. When I was a kid my pet mice lasted like two months and I kept good care of them too. I'm not as interested in the mad cow/mice disease as I am in the mouse longevity.

  4. this is truely scary by airbie · · Score: 5, Insightful

    because prions are more basic and fundamental than even germs/viruses. most modern methods of treating diseases and fighting virus involve disrupting the replication process of the virus/germs, usually by the means of inhibiting certain proteins. however prions themselves are malformed proteins that malform other good proteins. this mechanism is quite hard to stop because it is so simple, there is no complicated repoduction chain to disrupt like a virus. there is only one way to stop this chain, which is to basically burn the protein to a crisp.

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  5. Wrong university...butu you've got it mostly right by Anonymous Coward · · Score: 5, Informative

    This was done at UCSF, not UCSD. Read the article

    There are still a few people the dis-believe the prion theory of disease put forward by Pruisner. For those who aren't familiar with the subject, prions are essentially misfolded proteins that can induce their mis-folding by interacting with copies of themselves. So, if protein A become randomly misfolded into A', it can bump into other copies of A and induce them to form A'. In many of the disease cases, these misfolded proteins can form plaques or tangles which then disrupt or rupture and kill cells.

    While Pruisner's evidence for such a mechanism is more or less overwhelming there were still a couple people who didn't buy the story. The experiment talked about here (and I haven't seen the actual paper yet, but look forward to reading it) is rather difficult to do and is pretty much the last nail in the coffin of those disagreeing with prion theory. They do complain that the protein activities of the mutants were really low and that the mice used were not of the ideal strain buut this is missing the forest through the trees. As far as all of us whose opinions matter are concerned, the case is no more than closed and the pro-Pruisner side has won.

    BTW, I've heard Pruisner say that a lot of neurological diseases are really prion based...but that case is far from being closed...so keep your ears open for such discussions in the future.

    -Devon (who should disclose that he's a neuro grad student at UCSF, but works on neurogenetic diseases and not prions)

  6. A brief lesson on prions... by theluckyleper · · Score: 5, Informative

    Yes, I am a microbiologist, and I've done research on prions.

    Basically, prions are proteins which are able to act upon other proteins and thereby create functional copies of themselves (identical copies are not needed). BSE (mad cow disease) and CJD (essentially the human version) are caused by 'rogue' prions which destroy tissue by converting large quantities of protein into more prions. Prions are basically the most elementary form of an infectious disease (as they are simply protein, no genetic material required).

    Now, what these researchers have done is to prove that prions can spontaneously develop, without the need for viral or bacterial infection. Random changes in protein structure MAY result in prion creation. You needn't eat some mad cow (nor cannibalize some CJD gray matter) to contract CJD or some other prion-induced malady. Nor is a viral/bacterial infection required; the disease may develop spontaneously.

    Hopefully this makes sense... I've had a few too many Schooners (beer).

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  7. Only nukes are true WMDs by tepples · · Score: 5, Funny

    Great, now we have yet another form of weapon of mass destruction.

    Artificial prions are chemical weapons, just like VX, sarin, and other nerve agents. Unlike nuclear weapons, chemical weapons are technically not weapons of mass destruction because only a nuclear reaction can destroy mass.

  8. Shaking by wsherman · · Score: 5, Interesting
    Back when I was doing research on how individual proteins clump together to form the "amyloid" type of deposits found in diseases like Alzheimer's and diabetes, I had results from looking at the deposit formation in test tubes suggesting that deposit formation was promoted by shaking.

    The guy in charge of the project wasn't interested in pursuing the results because the intersection of protein dynamics and hydrodynamics wasn't somewhere he wanted to go.

    It will be interesting to see if they can develop anything more than handwaving explanations for how the shaking is causing the prions to change structure. Standard molecular dynamics simulations of proteins don't model mixing behavior of the water molecules surrounding the protein. Part of this may be due to the different time scales of the two phenomena.