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South Indian Frog Oozes Molecule That Inexplicably Decimates Flu Viruses (arstechnica.com)

Posted by BeauHD on from the flu-slashing dept.

An anonymous reader quotes a report from Ars Technica: From the slimy backs of a South Indian frog comes a new way to blast influenza viruses. A compound in the frog's mucus -- long known to have germ-killing properties -- can latch onto flu virus particles and cause them to burst apart, researchers report in Immunity. The peptide is a potent and precise killer, able to demolish a whole class of flu viruses while leaving other viruses and cells unharmed. But scientists don't know exactly how it pulls off the viral eviscerations. No other antiviral peptide of its ilk seems to work the same way. The study authors, led by researchers at Emory University, note that the peptide appears uniquely nontoxic -- something that can't be said of many other frog-based compounds. Thus, the peptide on its own holds promise of being a potential therapy someday. But simply figuring out how it works could move researchers closer to a vaccine or therapy that could take out all flus, ditching the need for yearly vaccinations for each season's flavor of flu.

8 of 114 comments (clear)

  1. Decimate? by Tovam · · Score: 5, Informative

    Decimate: Kill one in every ten
    That doesn't sound very useful.

    1. Re:Decimate? by rkordmaa · · Score: 5, Insightful

      That sounds very useful, finding mechanism where a finely tuned molecule happens to demolish a whole class of viruses could be a discovery on the level with antibiotics.

    2. Re:Decimate? by Opportunist · · Score: 5, Informative

      Which could be enough. Not to mention that decimate has gained a different meaning beyond "killing every tenth", with a more colloquial use it usually means "kills a portion of them" without going into detail how many.

      Antibiotics don't kill all bacteria either. That's why antibacterial soap, cleaning and laundry agents usually hurt more than they help, since they only kill the germs that are susceptible to antibacterial treatment, leaving the "superbugs" unharmed. Essentially what you do that way is breed them by playing natural selection, culling the weak ones to give the stronger ones more room and food to expand into.

      Why antibiotics work well in humans is that we have an immune system that doesn't care whether the bacteria are resistent to antibacterial treatment. What our immune system cares about is numbers. If too many bacteria come, it gets overwhelmed, at least for a time, and we get sick. If antibiotics kill off the majority of bacteria, the immune system can easily deal with what's left.

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  2. I have always wondered... by OpenSourced · · Score: 5, Interesting

    ...how all the technical and scientific capabilities of humankind cannot develop an antibody for a particular virus, but our immune systems do it in a couple of days, no sweat. Or rather, possibly lots of sweat, but they do it. One would thing that it would be possible to replicate the process somehow.

    Note: I understand that, in the case indicated in the article, it goes beyond that, offering some kind of general-purpose antibody, probably targeting parts of the virus cover that are more hidden, and usually don't mutate. But anyway. That we cannot design that peptide, and must rely on the blind watchmaker to find it for us, is a bit baffling.
     

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    1. Re:I have always wondered... by wierd_w · · Score: 5, Interesting

      proteomics is a very new field of study. It has only been very recently that we have been able to synthesize long dna and rna strands inexpensively, and even more recently that we could reliably induce quality insertion into a target organism for biosynthesis.

    2. Re:I have always wondered... by EvilSS · · Score: 5, Informative

      Antibodies, like all proteins, are pretty complex molecules. The binding sites in particular are very tricky. They need to be designed to bind properly to the target AND ONLY THE TARGET protein. This involves balancing physical geometry and electrical charges to match up with the target protein to get a correct fit and strong binding. This needs to happen at the atomic level, using amino acid building blocks. We don't even fully understand how our bodies do it yet. Think of it this way: we are still working towards building our first commercial, very basic nano machines. Our bodies (and all life for that matter) are filled with them. These machines, such as enzymes, are capable of doing amazing things, like building and re-arranging molecules at the atomic level. Each one customized to do a very specific task. We can hijack biology and genetics to make some of the things we want but as far as our technology goes, we are way, way behind nature.

      Right now our best option is to identify existing antibodies and isolate the genetic material the organism used to create it and using that to create GMOs to reproduce it.

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  3. Biodiversity by Anonymous Coward · · Score: 5, Insightful

    See, politicians, conserving biodiversity is not just hippy-happy-pro-Western-and-gay-culture-talk, potentially leading to the evils of godless democracy and missing the key authority figure of you.

  4. This may seem off topic, by jenningsthecat · · Score: 5, Insightful

    but this sounds to me like an additional call to, as a species, get our environmental practices under control and stop 'instinctifying' flora and fauna at a breakneck pace. With findings like this, I have to wonder how many illness-treating, disease-defeating compounds we may have sent into oblivion by killing off the plants, animals, and insects which produced them.

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