Why prions are so hard to destroy

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Nearly all organic material (like bacteria and viruses) is destroyed at temperatures above 60° Celsius. Some temperature resistant pathogens can survive slightly higher temperatures than this, but even the most hardy will be destroyed at temperatures above 150° Celsius.

But for prions these temperatures are hardly sufficient. They can survive being frozen, cooked, steamed, and even chemically treated with substances like formaldehyde and alcohol. Temperatures as high as 600° Celsius will not reliably kill them, and only in the 1000° Celsius range are they destroyed. At this temperatures, most *metals* will melt.

Why are prions so hard to destroy if they are chemically identical to the organic material inside our body already?

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Anonymous 0 Comments

The only thing you need to do to a living thing to “destroy” it is to kill it. Even viruses, which are debatably alive, have mechanisms in them which, when put out of order, make the whole not work. Because you’re dealing with complex mechanisms, something like 60C is enough to knock it out of order.

Prions are organic, but they aren’t alive. You can’t “kill” it any more than you can kill a rock. The only way to render it unable to infect is to physically break its shape, which is difficult.

As per [this manual](https://www.fao.org/3/a1001e/a1001e00.pdf), they really don’t routinely survive extreme heat, since it reports only “trace amounts of infectivity” and then speculates that it’s due to the inorganic skeleton of the prion surviving the process. Which makes sense, since if the shape remains, it might be able to still cause the same effect as an untreated prion.

Also, that paper goes on the detail that if moisture is added to the process, prions can be reliably destroyed at temperatures as “low” as 130C

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