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Prions Observed Jumping Species Barrier 214

Posted by timothy
from the only-applies-if-you-have-brain-tissue dept.
palegray.net writes "Nature is reporting on new findings that prions jump species barriers. Believed to be responsible for ailments such as Creutzfeld-Jakob disease and 'mad cow' disease, prions are thought to disrupt biological processes by causing normal proteins to fold abnormally. Researchers at the University of Texas Medical Branch in Galveston have observed infectious prions from hamsters causing abnormal protein development in mice, along with a range of other observations on prion actions in test tube environments. From the article: '... they also found that when a prion jumps species, it produces a new kind of prion. "This is very worrisome," says Claudio Soto, who led the research, published in Cell. "The universe of possible prions could be much larger than we thought."' Sounds like another good reason to donate your spare CPU cycles to projects like Folding@home."
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Prions Observed Jumping Species Barrier

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  • by damn_registrars (1103043) <damn.registrars@gmail.com> on Sunday September 07, 2008 @09:50PM (#24915443) Homepage Journal
    For those with access to the journal Cell [cell.com], you can view The Castilla, et al, paper [cell.com] online (this abstract should be available for all). The nature link in the summary goes to a write-up about the article, not the actual article itself.

    Those with subscriptions to Cell can also get the full text [cell.com], Full Text in PDF [cell.com], and the Supplementary Data [cell.com].
    • by g0dsp33d (849253)
      Haven't they proved this happening before by the fact that mad cow disease travels from tainted beef to humans? Or was that what they think caused the disease and they had no way of proving the jump with out risking someone's health?
      • by rrohbeck (944847)

        There was circumstantial (epidemiological) evidence that vCJD appeared mostly (or only, can't remember) in heavy beef consumers. Obviously, you can't *prove* it without experiments. But it has been proven that animals do get infected by feeding them prions from other species so it was assumed that this applies to humans too. Now, being able study the infection in vitro, they should be able to prove which prions can infect humans, and maybe come up with a test that doesn't require dissecting the brain.

    • The jumping accross species is known and documented for quite some time, specially regarding prions from mad cow disease.
      Similarily, I remember reading articles in 3rd year medicine(*) about difference in prion foldings between species (explain the initial slow development of inter-species spreading compared to intra-specie spreading) and emergence of newer folding pattern (after a while a new more efficient pattern emerges)

      I fail to see how this is news worthy, except maybe some lab trying to justify spend

      • DISCLAIMER: I have a science background but not in Medical science.

        More often than not, up to date university staff will be able to give students much more insightful tips on break through / newsworthy articles than, say, slashdot. Surprised? I am not.

        The fact that slashdot doesn't get that many *up-to-date* good science stories is, most probably, due to the lack of more up-to-date stories submissions. It certainly isn't due to lack of slow news days anyway...

        In any case, I often like slashdot better th

    • Now that I am at work, where I have access to cell, I can read the article and attempt to explain its significance. I will attempt to do this without violating copyright - although I see the work was supported by National Institutes of Health (NIH) funding, which requires that the papers be released to the public [pubmed.gov] (within a certain time frame).

      The paper mentions that the species barrier has been crossed by some prions (BSE) but not others (scrapies). They are looking for a way to show cross-species inter
  • by Anonymous Coward

    Nature is reporting on new findings that prions jump species barriers

    It's confirmed. Our planet (i.e. Nature) is sentient and into science journalism!

  • Oh No! (Score:2, Funny)

    by Anonymous Coward
    That's nothing. I have peons swarming my village.
    • I have Priuses swarming mine!

    • by couchslug (175151)

      "That's nothing. I have peons swarming my village."

      Heat and pressure have been observed to kill prions, and should work for your situation.

      Give it a try and post results!

  • "The universe of possible prions could be much larger than we thought."' Sounds like another good reason to donate your spare CPU cycles to projects like Folding@home."

    Can I donate my spare prions instead?

  • by fuzzyfuzzyfungus (1223518) on Sunday September 07, 2008 @10:06PM (#24915537) Journal
    While I certainly wouldn't want to get any of the prion diseases, they are all rather nasty, I find the existence of prions fascinating. They are arguably even less alive than viruses, though not by much, and yet they multiply(in a sense), and exist in all sorts of variants.

    It seems like any sufficiently complex system(biological proteins in this case), is at considerable risk of having something analogous to life spring up and cause trouble.
    • by jd (1658) <imipak@yahoo.cEINSTEINom minus physicist> on Sunday September 07, 2008 @11:01PM (#24915861) Homepage Journal
      Prions appear to exist in a space somewhere between crystals (they "multiply" in a way mot dissimilar to crystals growing and do not make anything "new" the way a virus would) and the lower end of what is considered "true" life. This suggests to me that there is a continuum and that the terms "living" and "non-living" are not descriptive of anything fundamental. If that is correct, then I suspect we will find that prions were an important stage in getting to what we call "life". However, it is not obvious as to how you'd get from a free-floating RNA/DNA strand and a prion to a living cell, so there must be other stages in between, if that indeed was the sequence. I suspect that a study of prions could yield such an additional step, but only if the researchers are willing to accept such a stage could exist.
      • by Hal_Porter (817932) on Monday September 08, 2008 @12:16AM (#24916229)

        Have you heard of Cairn's-Smith's clay theory of abiogenesis

        http://en.wikipedia.org/wiki/Graham_Cairns-Smith#Clay_theory [wikipedia.org]
        In simplified form, clay theory runs as follows: Clays form naturally from silicates in solution. Clay crystals, as other crystals, preserve their external formal arrangement as they grow, snap and grow further. Masses of clay crystals of a particular external form may happen to affect their environment in ways which affect their chances of further replication â" for example, a 'stickier' clay crystal is more likely to silt a stream bed, creating an environment conducive to further sedimentation. It is conceivable that such effects could extend to the creation of flat areas likely to be exposed to air, dry and turn to wind-borne dust, which could fall at random in other streams. Thus by simple, inorganic, physical processes, a selection environment might exist for the reproduction of clay crystals of the 'stickier' shape.

        There follows a process of natural selection for clay crystals which trap certain forms of molecules to their surfaces (those which enhance their replication potential). Quite complex proto-organic molecules can be catalysed by the surface properties of silicates. The final step occurs when these complex molecules perform a 'Genetic Takeover' from their clay 'vehicle', becoming an independent locus of replication - an evolutionary moment that might be understood as the first exaptation.

        Richard Dawkins said of this that he doesn't believe this particular theory of abiogenesis but something like this must have happened.

        He memorably said that one day a robot equivalent of Cairns Smith may note wryly that silicon based machines like him eventually took over from carbon based life like us that built them as tools in the same way that carbon based replicators took over from silicon based clay lifeforms that built them as tools.

      • However, it is not obvious as to how you'd get from a free-floating RNA/DNA strand and a prion to a living cell, so there must be other stages in between, if that indeed was the sequence.

        I'm no biologist, but I imagine viruses are one of those in-between stages...

        • by rve (4436)

          In my opinion, viruses have more in common with computer viruses than with life. They're not life, they're escaped pieces of 'code' that force a host to replicate and spread it.

          The process of selection has made some of these viruses more complex than the original fragment of RNA or DNA code, but they could not exist without life any more than computer viruses could exist without computers.

        • by Ihlosi (895663)
          I'm no biologist, but I imagine viruses are one of those in-between stages...

          Very unlikely. Viruses need the "higher" stages to reproduce. If the higher stages are not present, any virus that forms will be unable to reproduce.

      • by rve (4436) on Monday September 08, 2008 @12:59AM (#24916401)

        These prions are single molecules that have a harmful effect on the host. I believe the word 'toxin' is a better description.

        Prions don't self replicate, it's a substance that catalyzes (speeds up) the reaction of refolding an existing protein into another shape, not the formation of a protein out of other substances. If it catalyzed a different kind of reaction, you'd call it a toxic enzyme, not something on the continuum of life.

        • Re: (Score:3, Insightful)

          by lgw (121541)

          That's the best description I've heard so far. Bad prions are a particulary nasty biological toxin because they can survive conditions that destroy other biological toxins. They can apparantly pass through digestion repeatedly, aren't destroyed by an ordinary autoclave, and survive for a long time exposed to sun and oxygen. It's apparantly hard to sterilize medical equipment in such a way that prions are destroyed.

          The good news is that prion-based diseases are vanishingly rare. Avoid cannibalism and you

          • by rve (4436)

            That's because they're short, simple molecules, already in a 'relaxed' state. When you autoclave (boil) an egg, the proteins in the egg 'denature', they unfold to a more relaxed state. When you autoclave a boiled egg, the proteins don't denature any further. If you want to destroy the proteins in a boiled egg further, you'll have to turn up the heat far enough for the proteins to start to burn. At these temperatures, the equipment you are trying to sterilize in your autoclave will melt or burn.

            I once manage

          • Re: (Score:3, Insightful)

            by julesh (229690)

            The good news is that prion-based diseases are vanishingly rare. Avoid cannibalism and you're safe: so far meteor strikes are about as dangerous a threat, along with heart-attack induced by the stress of winning the lottery.

            Don't overestimate the threat of meteor strikes. While there have been a lot of near misses and property damage, there are apparently no recorded instances of somebody being killed by a meteorite since 1929.

            Just so you know.

        • by cartman (18204) on Monday September 08, 2008 @08:45AM (#24918411)

          Prions don't self replicate, it's a substance that catalyzes (speeds up) the reaction of refolding an existing protein into another shape...I believe the word 'toxin' is a better description.

          You're mistaken. Prions self-replicate by inducing other proteins to fold into prions like themselves. Prions thereby replicate and increase their numbers exponentially until they damage the organism. When symptoms appear, this process of exponential growth is already 95% complete and the organism will soon be dead. At that point, the organism is much more infectious because the number of prions is far higher than originally.

          Because prions replicate themselves, they bio-accumulate over time. Since organisms can "inherit" the prions of other organisms by ingesting them, the prions can accumulate across generations. Which means that you can feed cows to other cows continuously, and the number of prions in the cow population will increase over generations. It may take several generations of cow cannibalism before disease will become apparent.

          The prion hypothesis was interesting precisely because it proposed a mechanism of replication and infectivity which was not based upon DNA or RNA.

        • by zacronos (937891)

          These prions are single molecules that have a harmful effect on the host. I believe the word 'toxin' is a better description.

          Prions don't self replicate, it's a substance that catalyzes (speeds up) the reaction of refolding an existing protein into another shape, not the formation of a protein out of other substances. If it catalyzed a different kind of reaction, you'd call it a toxic enzyme, not something on the continuum of life.

          I would agree that they are a type of toxic enzyme, but I would also say they are a grey area in the spectrum of life. Prions don't self-replicate, but then neither do viruses. The key thing that (in my mind) makes prions something more than other toxic enzymes is the fact that their presence catalyzes a reaction that forms more of itself. I don't think most toxins actually increase concentration in the body over time (when left to their own devices), while this is indeed what we expect to see from disea

    • by oldhack (1037484) on Sunday September 07, 2008 @11:31PM (#24915987)

      It seems like any sufficiently complex system(biological proteins in this case), is at considerable risk of having something analogous to life spring up and cause trouble.

      Your name is not "Murphy" by any chance?

    • by irtza (893217)
      Well, I guess it all depends on how you define life... Most of these things are more semantic and issues because of our desire to fit things into categories. What's intersting is that prions in principle are similar to digestive enzymes in a way. Trypsin forms trypsin from trypsinogen in a self catalzying reaction. At the same time other enzymes may activate it as well. - Would you consider trypsin to be alive? The fact that prions exist as a pathology is interesting though. Furthermore, it points to t
  • by Anonymous Coward on Sunday September 07, 2008 @10:09PM (#24915559)

    So prions can make proteins into prions in other species, e.a. cross the species barrier? Big deal. We knew this in the nineties when the whole mad-cow disease was all over the news.

    I'm sure it has some scientific significance, but I think the real question is how (ingested) prions reach the central nervous system, where the damage is done. And why it takes so long or doesn't happen at all in most cases.
    Now that would shed some light on the amount of risk that eating a possibli infected piece of meat would pose. That would be news.

    • Re: (Score:3, Interesting)

      by Anonymous Coward

      i may have read the article wrong, but i'll give this a shot.

      you're right that we know that prions from cows can cause problems in humans. but i think what the article said is that it creates a new kind of prion as well. so where there used to be just one mis-folded protein messing with you, now there are two mis-folded proteins messing with you, and each is mis-folded in a different way and can do a different thing to you. so while you used to just have apples, now you have apples and oranges to deal with.

    • by arth1 (260657)

      Not only did we know it could affect humans, but it's been apparent for a long time now that the Mad Cow Disease is a very close relative to Scrapie in sheep, and that one can transform to the other.

      Which is precisely why there's a ban on using sheep remnants in cattle feed.

    • by julesh (229690)

      So prions can make proteins into prions in other species, e.a. cross the species barrier? Big deal.

      The summary's wrong. Yes, we've known this for ages. What's new is we have a nice, fast, reliable way of studying without actually infecting animals, which could help us answer the important questions, like 'can this particular prion infect humans?'

  • I guess prions take the Folding@Home idea a bit too literally.

  • The science of fear. (Score:2, Interesting)

    by Anonymous Coward

    I work for one of Claudio Soto's former PhD students. From my brief skimming of this paper, it seems to be a simple proof-of-concept transmission between mice and hampsters. The discussion section, like a lot of science, is pure speculation - logical, but no need for slashdotters to scream "OMG we're all going to die!"

    I'm an avid MN deer hunter (and consumer...) and I've done a significant amount of work with PrP infected mice. While not worried about going crazy and having my brain melt in 15 years, I h

  • Ailment? (Score:5, Informative)

    by ghoti (60903) on Sunday September 07, 2008 @10:33PM (#24915691) Homepage

    I'm sorry, but Creutzfeld-Jakob disease is a bit more than an "ailment." It's deadly and incurable. I think a slightly stronger word would be in order.

  • by jsse (254124) on Sunday September 07, 2008 @10:39PM (#24915721) Homepage Journal
    Prof. Charles Francis Xavier:
    "This process is slow, and normally taking thousands and thousands of years. But every few hundred millennia, evolution leaps forward."

    "We called them, X-Prions"
  • to the old saying "you are what you eat"
  • Worrisome for who? The cannibals? Stop eating brains!

    • Stop eating brains!

      But if I do that, how will I learn things?

      *points to sig for the slow among the readership*

  • by transporter_ii (986545) on Sunday September 07, 2008 @10:44PM (#24915767) Homepage

    I couple of years back, I did a lot of reading on Mad Cow. There were so many examples of it jumping the species barrier...and some of them many, many years old.

    Here is an example from 18 years ago:

    -=-=-=

    http://www.highbeam.com/doc/1G1-111779850.html [highbeam.com]

      WASHINGTON -- Eighteen years before last week's first confirmed case of mad cow disease in the United States, investigators concluded that an epidemic of a brain-wasting disease on a Wisconsin mink farm was probably caused by a malady similar to mad cow disease.

    The Wisconsin farmer had fed his mink a steady supply of "downer" cows -- too sick or injured to move on their own -- like the one that tested positive for mad cow disease in Washington state last week. On Tuesday, the Department of Agriculture banned such animals for human consumption.

    Long before the USDA action, the mink industry began discouraging farmers ..

    -=-=-=

    It is basically that anyone who did a little study would know that it could jump the species barrier...but it just can't do that until some people in white coats tell us it can do that...then it can.

    transporter_ii

    • by tloh (451585) on Monday September 08, 2008 @12:34AM (#24916313)
      mod parent up. I did some reading last year on Cronic Wasting Disease (CWD was mentioned in the article) for my infectious disease class and examples like the outbreak at the mink farm just mentioned was very prevalent in available literature. I think most people are getting the wrong idea because the article is badly written for a non-technical audience. The novelty seems *not* to be that prions can cause cross-species infections, but that it has been demonstrated in vitro (by way of "protein misfolding cyclic amplification (PMCA) protocol") in such a way that elucidated some details (multiple forms as revealed by novel strain properties) that were not apparent before. This is interesting *not* because it is a ground breaking new discovery, but because it serves as a starting point for further studying cross-species prion interaction from a different perspective using different techniques.
    • by julesh (229690) on Monday September 08, 2008 @04:57AM (#24917243)

      Uhuh. The summary is just wrong, is what's going on here. If you read the article, what it's actually about is a new way to study prions in vitro and test them to determine whether there's a possibility of them crossing a particular species barrier.

      Which is, when you think about it, a very useful test to have available.

  • Scary (Score:5, Interesting)

    by Pedrito (94783) on Sunday September 07, 2008 @10:53PM (#24915813) Homepage

    It made me wonder, if it changes when it jumps species, maybe prion diseases are something new, so I did some quick checking on Wikipedia. I didn't track down more stuff yet, but I plan on following up. I didn't realize this, but it appears that a lot of prion diseases are fairly recent developments. Scrapie showed up in 1732, Bovine Spongiform Encephalopathy in the 1800s, CJD showed up around 1920, Kuru in 1957, Chronic Wasting Disease in 1967, Feline Spongiform Enecephalopathy 1990.

    And these are more than half of the diseases caused by prions, I believe. That's more than a bit disconcerting.

    • Re:Scary (Score:5, Insightful)

      by rrohbeck (944847) on Monday September 08, 2008 @12:05AM (#24916177)

      I didn't realize this, but it appears that a lot of prion diseases are fairly recent developments.

      People didn't eat as much meat as they do today, didn't live as long, and they certainly didn't feed their livestock with slaughterhouse waste. The latter is what got prions into the food chain in significant amounts.

    • Re: (Score:2, Insightful)

      by registrar (1220876)

      Smallpox had been around for thousands of years, but it was only in the last few centuries that people identified it as being distinct from chickenpox, measles and other poxes. It doesn't prove that there's been a proliferation of poxes, just a lot more classifying going on.

      That said, our changing living patterns do expose us to new diseases (see sibling post) like BSE, SARS and HIV---all depending on who you mean by "us". There's truth in what you observe, but it's not a huge deal because that same cha

      • by Pedrito (94783)

        There's truth in what you observe, but it's not a huge deal because that same change in living patterns means that we know what caused it and what to do about it. Life expectancy has gone up dramatically despite the introduction of new diseases.

        True, but if prion diseases are starting to pop up out of nowhere then I'm a bit concerned, because the ones that have been around for a while, like CJD, have no cure.

  • by nido (102070) <nido56@ y a h o o . c om> on Sunday September 07, 2008 @10:53PM (#24915817) Homepage

    ... Mark Purdey [markpurdey.com] was, of course, the British beef farmer who had a different theory about Mad Cow. In the 80's the British government required all cattle to be dosed with an Organo-phostate pesticide, to combat a warble fly epidemic (these bugs punch holes in cattle skin, making the hides less suitable for leather seats).

    Purdey was an organic farmer, and sued to protect his right to keep synthetic pesticides away from his herd. He won. A few years later Chernobyl went off, and some time after that the first Mad Cow epidemic occured. Purdey's cows were mostly immune. He had a few mad cows, but these were mostly transplants to his herd which had, presumably, been dosed with the pestacide.

    As the years went by, Purdey turned into a scientist himself, doing the research that the british government wouldn't do because of their potential liability in having caused the mad-cow epidemic (by require farmers to poison their herds).

    Basically, the pesticide used chellated (removed) copper from the treated body. Somehow manganese substitutes for copper, but it isn't a good subsitute. The radioactive fallout from Chernobyl didn't help things either. It's been years since I first read Purdey's site, so I don't remember the details.

    He commented that the Mad Cow in Washington (the northwest state) came from a copper-deficient pasture in Canada, into an area where quite a bit of nuclear weapons research had been done in decades past. The mad deer in Colorado also occupy a site with extensive radiologic environmental poisoning.

    So basically, Purdey's theory is that prions are an effect of environmental poisoning, not the cause of Mad-Cow-esque disease.

    Purdey is deceased now (brain cancer?), but his site's still live. Definitely recommended reading.

    • by timmarhy (659436) on Sunday September 07, 2008 @11:15PM (#24915917)
      sounds like nonsense to me, just a crack pot theory piecing bits together combined with 1/2 truths.
      • by Reziac (43301) * on Sunday September 07, 2008 @11:25PM (#24915967) Homepage Journal

        Yes, but now I'm wondering... DNA can be damaged/mutated by environmental factors; proteins can be damaged by chemicals (when I was in college, we used the crude method of boiling proteins in a saturated lye solution to break them down into their various amino acids); why should prions be immune?

        Which says nothing pro or con re this Purdey fellow's theory of the origin of BSE; he could be dead-wrong on that, yet correct as applied elsewhere. Or he may be completely off-base in every way, yet we should still look at *what* causes prions to "fold wrong"; who knows what we'll learn?

      • While Mark Purdey may not be right about organophosphates (although they may have been a contributing factor) he is (was) correct that the scientific orthodoxy about CJ-like diseases is wrong.

        Although prions are not directly my area of research, I have been an interested observer. It is my belief that the idea tha prions are a self-reproducing pathogenic protein (the idea that won Stanley Prusiner a Nobel Prize) is fundamentally wrong. So called "prion diseases" do, in fact, have have nucleic acid genome.

    • by tfoss (203340) on Sunday September 07, 2008 @11:58PM (#24916147)

      Purdey's theory is that prions are an effect of environmental poisoning, not the cause of Mad-Cow-esque disease.

      First off, those two statements are unrelated. Prions can cause TSEs regardless of if copper or manganese from the environment causes them. Secondly, it is pretty well accepted by the scientific community that prions are the cause of TSEs. You can infect animals with PrP-Sc (the misfolded form of the prion protein (PrP-C being the normally folded version) and cause TSE. If you knock out the PrP protein, mice are not susceptible to PrP-Sc.

      What causes the first misfolding of PrP-C to PrP-Sc is unknown (unfortunately), and it is clear that PrP-C has copper-binding repeats, so an effect of Cu on the protein is a very likely possibility.

      -Ted

    • by taj (32429)

      Having lived in the Colorado front range, some of the comments sounded odd enough that I looked at his site and try to read between the lines - some of the comments blur the lines of politics and science. His copper and magnanese observations may be pointing to something that will later make sense in a more refined theory.

      Mark sounds like he was an intesting person. It looks like he itching to know if a copper supplement helped.

    • by cartman (18204)

      I read some of Purdey's stuff.

      I'm always extremely skeptical when a scientific outsider claims that his scientific discoveries are being suppressed by conspiracies and totalitarian forces.

      Not to mention, Purdey's hypotheses seem to be based on nothing more than coincidences and selective correlations.

      But Purdey seems to pay attention only to some correlations. He ignores the correlations which would destroy his hypothesis. For example, he ignores that Kuru disease (a prion disease affecting humans) ha

  • Is that surprising ? (Score:3, Interesting)

    by aepervius (535155) on Sunday September 07, 2008 @11:20PM (#24915939)
    Many of the proteins of the mammals are qu7ite in common except sometimes for a few details. If those few details make no difference to the attack site of the prion, it ain't that surprising that other similar brain protein can similarly badly in other mammals. Sooooo we should simply ban utterly to feed other dead mammals protein to other specy which are for human consumption (cue the sales of meat carcass into pet food....).
  • Just build a giant wall between our species and the rest. Use lots of high tech things like cameras, UAVs, and the like. That'll work.
  • by vrjim (1287740)
    Become a vegetarian and loose the risk of contracting a scary prion disease from your food. Prion diseases are awful- I'd take an STD or physical handicap any day over one of those. Now I understand that the USA only randomly checks 1% of cattle for mad cow disease. Since we HAVE had cattle found with it before that stands to reason that cattle with prion diseases have made it into the food supply. The scariest part is these prion diseases can have incubation periods in both cattle and humans for many year
    • by Weedlekin (836313)

      "Become a vegetarian and loose the risk of contracting a scary prion disease from your food."

      The incidence of that scary prion disease in humans is extremely low. Even the the UK, where 400,000 infected cattle entered the food chain in the 1980s, has only had 193 cases (suspected and confirmed) over 25 years in a population of over 60 million people, and their figures are more accurate than anyone else's because they're the only country to have instituted mandatory reporting of cases with symptoms that even

  • by SuperBanana (662181) on Sunday September 07, 2008 @11:52PM (#24916123)

    Sounds like another good reason to donate your spare CPU cycles to projects like Folding@home."

    So the public is donating a lot of computing time and electrical energy. What does the public get back?

    If Folding@Home goes towards lining the pockets of a university endowment or a drug company's coffers, count me out. If the research product is required to be free from patents, and available for public good...full speed ahead. Somehow, I seriously doubt that any successful results will be freely available.

    • by julesh (229690) on Monday September 08, 2008 @05:07AM (#24917305)

      So the public is donating a lot of computing time and electrical energy. What does the public get back?

      If Folding@Home goes towards lining the pockets of a university endowment or a drug company's coffers, count me out. If the research product is required to be free from patents, and available for public good...full speed ahead. Somehow, I seriously doubt that any successful results will be freely available.

      The project is run by a non-profit company. Results are routinely made public. I don't see any reason to be concerned here.

    • Re: (Score:2, Informative)

      by padre999 (1359905)
      Ever heard of world community grid?
      http://en.wikipedia.org/wiki/World_Community_Grid#Outreach [wikipedia.org]
      "Also, as part of its commitment to improving human health and welfare, the results of all computations completed on World Community Grid are released into the public domain and made available to the scientific community."
  • idle cpu? (Score:4, Insightful)

    by stm2 (141831) <sbassi@gene[ ]gitales.com ['sdi' in gap]> on Monday September 08, 2008 @12:04AM (#24916167) Homepage Journal

    There is not such a thing as "spare CPU cycles" since when you run a *@home program, CPU power consumption pikes.
    In a laptop, when running any CPU intensive distributed program, battery level is stuck since all the power goes to the CPU instead of charging the battery.

    • by compro01 (777531)

      I dunno what laptop you have, but the manufacturer did not include a large enough power brick. Every laptop I have seen or owned will charge even when being run at full tilt.

  • I for one welcome our new micro overlords.

    All hail the Prions Of Ori!

  • an even better reason to go vegetarian. Or at least not eat beef.

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