Their ability to resist heat has been greatly exaggerated. The kernel of truth is that some sterilization procedures are insufficient to eliminate them and that definitive guidelines have not been fully agreed on. Common folklore translates this into "they are impervious to heat."

Please describe the process by which a prion is rendered harmless at a mere 100C. Denaturing a protein generally requires a lot more.

> Denaturing a protein generally requires a lot more .. than 100C

Nope. Protein generally denatures at lower than 100C / boiling point.

That's the principle of Sous Vide, not that you should use Sous Vide to sterilise anything, but the protein in egg white denatures at 60-80C.

http://www.scienceofcooking.com/eggs/eggs_sous_vide.htm

And in meat it's similar, 50-70C http://www.mpip-mainz.mpg.de/Sous_vide_cooking

If you doubt it, stick your hand in water at 80C and see what happens.

Prions don't degrade at the boiling point: http://www.microbiologyresearch.org/docserver/fulltext/jgv/8...

Sure, though that's entirely different from the grandparent post's statement about "Denaturing a protein generally", which happens well below boiling point.

Where did I claim they were rendered harmless at a mere 100C?

Heat will destroy prions, but you need far higher temperatures for longer periods than normal.

One could think of them as edge cases in the "program" of protein folding and therefore a 'bug' of sorts.