The typical sponge-like brain damage seen in prion diseases may not be observed.
June 10, 2022
I found a fascinating, and I believe very important paper from September 2006 in the Journal of Virology. The paper is entitled: Modulation of the Unfolded Protein Response by the Severe Acute Respiratory Syndrome Coronavirus Spike Protein.
What this paper demonstrates is that the Spike Protein alone induces Endoplasmic Reticulum stress and the Unfolded Protein Response. However, it selectively modulates gene expression so that PROTEIN FOLDING IS ENHANCED, WHILE SIMULTANEOUSLY DISABLING ER STRESS-INDUCED APOPTOSIS.
What does this mean? This raises the possibility that the accumulation of nascent and unfolded SARS-CoV proteins in the lumen of ER might rapidly exceed its folding capacity, thereby perturbing the normal cellular function of ER. In other words, the ER is overloaded and starts to make lots and lots of proteins which results in folding errors and misfolded proteins being expressed as the cell does not kill itself, as it is supposed to do when the ER gets overloaded by a pathogen.
(The following link is on a site with an expired SSL, I downloaded the paper and experienced no issues.)
THE SPIKE PROTEIN CONTAINS PRION-LIKE DOMAINS
A paper from January, 2022, is the most complete analysis of the Prion-like domains of the Spike Protein. They found that although different β-CoV members contain PrDs in the S proteins, SARS-CoV-2 IS THE ONLY MEMBER (WILL MIRACLES NEVER CEASE) that has a PrD in the RBD of the S protein that binds to the ACE2 receptor employed for host-cell entry. Furthermore, they discovered specific amino acids (Q474, N481, Q493, Q498 and N501) that enable the prionogenity of the SARS-CoV-2 RBD that directly interacts within ACE2.
Notably, with more precise mapping of PrDs within these proteins, they found a striking difference in their localization, with SARS-CoV-2 BEING THE ONLY VIRUS (DIDN’T SEE THAT ONE COMING) with PrDs identified within the RBD of the S protein.
WHAT DOES THIS HAVE TO DO WITH PRION DISEASE?
MEET THE ANCHORLESS PRION
Fascinatingly, in experiments from 2010, using homozygous transgenic mice expressing TWO-FOLD MORE ANCHORLESS PrP, scrapie infection induced a new fatal disease with unique clinical signs and altered neuropathology, compared to non-transgenic mice expressing only anchored PrP. Furthermore, electron and light microscopic studies in infected transgenic mice demonstrated several pathogenic processes not seen in typical prion disease, including CEREBRAL AMYLOID ANGIOPATHY. The findings were similar to certain human familial prion diseases as well as to non-prion human neurodegenerative diseases, such as Alzheimer's disease.
THE OVERSTRESSED ER, COMBINED WITH A MASSIVE AMOUNT OF FREE SPIKE, INDUCES THIS NEW TYPE OF PRION DISEASE
I believe we have now bridged the all too obvious chasm we have been suspended over these past two and a half years. Prions. Amyloids. This hypothesis may explain the neurodegeneration we have been observing, and may explain the dramatic increase in sudden deaths, as the brain stem may be more severely affected.