THE SPIKE PROTEIN OF SARS-CoV-2 INDUCES A SYSTEMIC AMYLOID PRIONOPATHY
March 29, 2022
“We shall not cease from exploration
And the end of all our exploring
Will be to arrive where we started
And know the place for the first time.”
--from Little Gidding by T.S. Eliot
When I first began researching the Spike Protein of SARS-CoV-2, I believed it was virtually a Prion, and capable of inducing Creutzfeldt-Jakob Disease (Mad Cow Prion Disease). As it turns out, I believe that observation could be considered as viewing a tree in a massive forest.
After almost two years, I now believe that the Spike Protein is a “Universal Prion” capable of inducing a systemic Proteinopathy. It all begins with the “Prion” (Spike Protein) invading the body via the Endothelium.
This has precedence.
Vascular-Associated Dendritic Cells (VADCs), a network of which is known to be present in arterial vessels of healthy individuals25 are also related to atherosclerotic lesions with a possible role of T-cell activation.27 Dendritic cells can migrate via the blood to the spleen or via lymph into lymph nodes where they are known as interdigitating cells. Close contact between VADCs and macrophages suggest a possible interaction between these cell types processing immunological information. VADCs may also migrate across vessel walls (to eg, lymphoid tissue). Thus, they might serve as common link between pathogenic events in the periphery as well as in neuroinvasion of prion diseases.
Immunocompetent cells of vessel walls may participate in PrPSc production (analogously to follicular dendritic cells) and/or transport. As these cells might be in contact with both neural and extraneural tissue, our results raise the possibility of mobile cell-related spread of PrPSc and infectivity.
The conformational diseases, linked to protein aggregation into amyloid conformations, range from non-infectious neurodegenerative disorders, such as Alzheimer's disease (AD), to highly infectious ones, such as human transmissible spongiform encephalopathies (TSEs). They are commonly known as prion diseases. However, since all amyloids could be considered prions (from those involved in cell-to-cell transmission to those responsible for real neuronal invasion),
This is the case of the Spike Protein. When Spike Protein is added to platelet-poor plasma (PPP), with and without thrombin, a major increase in dense anomalous clotted deposits, with an amyloid nature, were noted (referred to as amyloid deposits).
Scanning electron- and fluorescence microscopy revealed large, dense anomalous and amyloid masses in WB and PPP of healthy individuals where spike protein was added to the samples. Mass spectrometry confirmed that when spike protein was added to PPP, it interacts with plasma proteins, resulting in fibrin(ogen), prothrombin and other proteins linked to coagulation, to become substantially resistant to trypsinization, resulting in less fragments. Flow analysis confirmed that microclots may impair blood flow. Here we suggest that, in part, the presence of spike protein S1 in circulation may contribute to the hypercoagulation in COVID-19 positive patients and may cause severe impairment of fibrinolysis.
So, we have an explanation for hypercoagulation – and induction of Prion disease. The hypercoagulation is of note, as plasma of COVID-19 patients also carries a massive load of preformed amyloid clots. I believe this may explain the large clots being found by coroners and pathologists.
It has been hypothesized that AA amyloidosis is a factor causing systemic complications after coronavirus disease. The consequences of COVID-19 infection are surprisingly similar to the clinical picture that is observed in AA amyloidosis. A high level of SAA IS EXCLUSIVELY A BIOMARKER OF COVID-19.
THE CANCER CONNECTION
In fact, mutant p53 (which is downregulated by the Spike, and I now believe it is being misfolded by the presence of the Spike into amyloids) is highly prone to misfolding and frequently resides inside the cell as large aggregates, causing loss of physiological function of the tumor-suppressor protein. The resulting functional loss of p53, including amyloid formation leads to UNHINDERED CANCER PROGRESSION.
Therefore, it should come as no surprise that we are seeing Prion-like neurodegenerative disorders emerge from the actions of the Spike Protein. The most conspicuous feature of many neurodegenerative disorders, including Alzheimer's, Parkinson's, and Huntington's disease, is the occurrence of protein aggregates in ordered fibrillar structures known as amyloid found inside and outside of brain cells.
Additionally, emerging evidence suggests that many common forms of cardiomyopathy may belong to proteinopathy, which may explain a portion of the sudden cardiac deaths.
I believe we can explain the entire pathology of the Spike Protein by viewing it as a systemic proteinopathy. My initial thought that it induced principally Creutzfeldt-Jakob Disease was from seeing the mechanism, but not understanding the immense amyloid forming and aggregating powers of the Spike Protein.
Protein Misfolding, Amyloid Formation, and Neurodegeneration
Prion-like p53 Amyloids in Cancer
Hypothesis: AA amyloidosis is a factor causing systemic complications after coronavirus disease
Proteinopathy-induced neuronal senescence: a hypothesis for brain failure in Alzheimer's and other neurodegenerative diseases
SARS-CoV-2 spike protein S1 induces fibrin(ogen) resistant to fibrinolysis: implications for microclot formation in COVID-19
The ubiquitin-proteasome system in cardiac proteinopathy: a quality control perspective
Disease-Associated Prion Protein in Vessel Walls
When amyloids become prions