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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For a true ELI5 answer, proteins aren’t destroyed when heated or treated chemically. They’re still there, they just aren’t in the right shape to do what they need to do for life/infectivity.
Imagine a normal protein as a ball of string or twine, thar you get from the store. It’s pretty easy to mess up by unwinding or cutting, and you’re unlikely to get it back exactly as it was. A prion is a ball of string where it’s all tangled up and knotted, and very very difficult to unwind, even cutting strands doesn’t unwind the thing.
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