Summary: A single genetic change provided complete protection against an invariably lethal dementia.

A naturally occurring variant of the human prion protein completely prevents prion disease (2015)

…mice expressing only PrP V127 were completely resistant to all prion strains, demonstrating a different molecular mechanism to M129V, which provides its relative protection against classical CJD and kuru in the heterozygous state. Indeed, this single amino acid substitution (Gright arrowV) at a residue invariant in vertebrate evolution is as protective as deletion of the protein.

Reported as: Cannibalism and the Resistant Brain

…replacing a glycine with a valine at position 127 is associated with resistance to kuru…

“…we were surprised that the mice were completely protected from all human prion strains, the result could not have been clearer or more dramatic.”

The result is quantized energy-dependent and food energy is the link to the fixation of the amino acid substitution in the context of autophagy via the pheromone-controlled physiology of reproduction, which typically biophysically constrains viral latency and all pathology.

Fixation of the achiral amino acid glycine in position 6 of the gonadotropin releasing hormone decapeptide has been linked to viral latency and all morphological and behavioral phenotypes in all vertebrates via invertebrate model organisms of how olfaction and pheromones control sympatric speciation.

But see for comparison:

Collinge added: “This is a striking example of Darwinian evolution in humans, the epidemic of prion disease selecting a single genetic change that provided complete protection against an invariably lethal dementia.

Leave a comment

Your email address will not be published. Required fields are marked *

error: Content is protected !!