Yes, it is safer. Basically what we discovered in the 90s is that cannibalism (an animal eating others of its species) has a relatively high chance of leading to protein mis-folding in that animal, producing prions. Those prions can then cause additional mis-folding producing more prions, this time in a very direct way that is unrelated to who consumes the meat.
So pig > pig or cow > cow is known to produce prions. I believe it's also somewhat proven that, say, pig > cow > pig does not produce prions in the same way. However, insect digestion is very different from vertebrate digestion, so it's not necessarily safe to assume that pig > cow > pig being safe means that pig > insect > pig would also be safe. However, it does prove that pig > insect > cow > pig would still be safe - the insects don't add a risk in themselves, we're just not certain that they eliminate the risk the same way vertebrate digestive systems do.
While cannibalism is related to transmission in some cases I don't understand it to have anything to do with prion formation in and of itself. See scrapie for example. While highly contagious the underlying cause of scrapie is typically (afaiu) genetic and transmissible through the environment over fairly long periods of time.
Which is to say that things are likely even a bit worse than you seem to be making out.
Yeah and to be honest the research on it is still at the start. Maybe with the advances in protein folding computational research we'll be able to understand this better
Because that's the biological equivalent of that catastrophic bug that only happens in very weird and very specific conditions
My understanding is they don't actually simulate or calculate (meta)stable states of proteins, but rather extrapolate on known folds of experimentally confirmed proteins (basically peeking at what types of folds are found in similar sequences in other proteins. then known as homologous proteins).
How proteins get folded, unfolded, refolded etc depends on the exact cellular or vacuolar environment.
AlphaFold isn't trained on the environment, it only sees the known mappings from genetic sequence to protein structure. It is patently unaware of any environmental aid or frustration in correctly folding a protein.
An incorrectly folded protein structure (putative prion structure) and its correctly folded structure share the same genetic sequence. AlphaFold is effectively blind, it was just trained on correctly folded proteins with known structure.
Unless future versions of alphafold use ML to speed up actual QM or molecular modelling calculations
I don't see how alphafold can help enumerate all potential misfolds of all proteins generated or preserved in an animal of species A and consumed in an animal of species B, and calculate all possible ways a misfolded protein from A may act as a prion in B.
Its only safer because of dilution - insects are less likely to have proteins that a prion can induce to misfolding.
But unless it is demonstrated that insect digestive systems have some magical enzyme that can do what autoclaves can't, that is break down prions, then it cannot be assumed safe.
So pig > pig or cow > cow is known to produce prions. I believe it's also somewhat proven that, say, pig > cow > pig does not produce prions in the same way. However, insect digestion is very different from vertebrate digestion, so it's not necessarily safe to assume that pig > cow > pig being safe means that pig > insect > pig would also be safe. However, it does prove that pig > insect > cow > pig would still be safe - the insects don't add a risk in themselves, we're just not certain that they eliminate the risk the same way vertebrate digestive systems do.