Apparently prions are pretty hard to kill off, the sterilization procedures are pretty long. https://www.cdc.gov/prions/cjd/infection-control.html
"In 2015, researchers at The University of Texas Health Science Center at Houston found that plants can be a vector for prions. When researchers fed hamsters grass that grew on ground where a deer that died with chronic wasting disease (CWD) was buried, the hamsters became ill with CWD, suggesting that prions can bind to plants, which then take them up into the leaf and stem structure, where they can be eaten by herbivores, thus completing the cycle. It is thus possible that there is a progressively accumulating number of prions in the environment."
Dark dreams of a planet's biosphere irreversibly becoming utterly hostile to organisms that use neurons to function, through accumulation of immortal zombie nanoparticles that convert more and more proteins to their side.
OMG.
I recall watching a PBS show on prions back in the 90s where they tried to destroy them in various ways : burning, burying, etc, and they were extremely difficult to destroy.
The moose population there has increased nearly 10x since 1960. In the 2020 hunting season, 3900 moose were taken. That is more than the entire population in 1960. So it seems like the people of NB having been eating increasing amounts of moose over the years.
It will be interesting to see if these unlucky folks are moose eaters.
Edit: Link - https://www.cbc.ca/news/canada/new-brunswick/2020-new-brunsw...
Aren’t proteins generally easy to denature? Isn’t that what most cooking does? And what alcohol does?
Prions are generally much more stable and can revert back to dangerous form once denaturing conditions change back. It takes a lot more to denature them irreversibly than it does most proteins. This stability is part of what makes them so dangerous and difficult to remove.
Indeed I'd imagine that almost definitionally prions must be difficult to denature. Since they are non-living and therefore have no way of "seeking out food," durability is the only way they can compete for reproduction. That is they can only become infectious if their resistance to denaturing was sufficiently high to resist environmental damage until their next target comes around.
https://www.scientificamerican.com/article/surgical-exposure...
However there is a difference between a denaturing process and a lysing (breaking) process, meaning that the actual covalent, chemical bonds between the component amino acids that make up a protein are broken. This bond is called the peptide bond, and they are extremely stable, and to break them without enzymes requires some crazy conditions like strong acids or bases and high heat and long periods of time. There is a class of enzymes called proteases that catalyze and speed up this breaking-down process, which is what cells use to digest and break down proteins.
So, yes, it is protein denaturation. But it's a very specific denaturation endpoint that not all proteins are capable of, and it's such a favored endpoint that even heating won't quantitatively destroy it (and heating could make it worse by fragmenting it into a bunch of smaller sheets).
[0] Incidentally, this denaturation is probably also used by cells in a productive fashion, it's pretty likely IMO that your melanin cells use these sheets to template melanin formation and sequester away the melanin molecule (the melanin precursor is highly toxic). I would link to the paper, but I think all of the data have been essentially cherry picked from shittily-done experiments, even though I think their conclusion is correct -- I have personally repeated the experiments "correctly" and reached the same endpoints in one shot without cherry picking (unpublished for my experiment, also n == 1) -- so I don't want to draw more unhealthy attention to the paper until someone else does the experiment "correctly".
[1] how does this happen? It can happen either due to a mutation that destabilizes the parent, well-folded protein, or, just by bad luck / time. Mutation examples: Fatal Familial Insomnia, non-variant CJD. Bad luck/Time example, insulin in a bottle in a fridge will turn into white flecks (these are sheets). The time at which this happens is highly variable (luck). You can accelerate this by agitating the bottle, and creating an air-water surface that catalyzes the denaturation of insulin. Also note, that insulin is not the protein in sheets in diabetes :biology trollface: (the insulin situation is strictly in vitro, and pH-dependent, as far as we can tell)
1. Theoretically speaking, yes. And there's probably a biological protease that does it in the the body. Last I checked, it's still unidentified; my money is on Insulin-Degrading Enzyme.
2. It's more complicated than that. If you just buy an off the shelf protease, it probably won't work, because those are used to cutting up floppy bits of peptide sticking out of a protein, so to get there you would need to pull the sheet apart ribbon by ribbon first to be effective.
3. Given enough time, though, the ribbons ARE in equilibrium between being on/off of the ends of the sheet, so a protease could randomly catch the ribbon at the right time. But the equilibrium is so low, that your protease would probably self-digest faster than it takes apart the flat protein sheet.
Is there a way to somehow pack chemical or electrical energy into these highly favorable stable endpoint configurations, and release it?
If you don't mind: what's the most likely source of this new disease? What's the worst case scenario, and how likely is it to play out?
Aside from that I think it's irresponsible for me to comment much on it since there is so little information in OP.