The Now Ubiquitous and Fatal White Clots: A Prion Disease of the Blood?

Could the relationship between Heparin, Prions and Spike Proteins be inducing a fatal Prion Disease in the blood?

Many readers may be aware of John Campbell's recent work discussing the white clots which have been observed in autopsies. He correctly states that these must be discussed. I have been searching for mechanisms which could induce such disastrous structures to be formed within the blood. What I have discovered is both fascinating and disturbing.

These clots should be looked at as a possible new form of Prion Disease. However, this is not the heretofore neurodegernative type of Prion Disease. This is a radically new form of the disease - on that affects the blood. I shall now explain how this may occur.

Heparin has long been known to cause White Clot Syndrome. Indeed, as far back as 1985.

The Authors report a new iatrogenic complication of preventive or curative standard heparinotherapy. This so called "white clot syndrome" or "Heparin associated thrombocytopenia and thrombosis" is an anatomico-clinical entity characterized by severe, multiple, recurrent, arterial and/or venous thromboembolic accidents which are sometimes fatal.

The white clot syndrome or heparin associated thrombocytopenia and thrombosis (WCS or HATT) (26 cases)
https://pubmed.ncbi.nlm.nih.gov/3831153/

Now, where this gets really interesting is that Heparin is also able to bind to the Receptor Binding Domain (RBD) of the Spike Protein.

The SGP from Delta and Omicron showed higher affinity (KD) to heparin than the WT SGP. Competition SPR studies using heparin oligosaccharides indicated that binding of SGP RBDs to heparin requires chain length greater than 18. Chemically modified heparin derivatives all showed reduced interactions in competition assays suggesting that all the sulfo groups in the heparin polysaccharide were critical for binding SGP RBDs with heparin. These interactions with heparin are pH sensitive. Acidic pH (pH 6.5, 5.5, 4.5) greatly increased the binding of WT and Delta SGP RBDs to heparin, while acidic pH slightly reduced the binding of Omicron SGP RBD to heparin compared to binding at pH 7.3. In contrast, basic pH (pH 8.5) greatly reduced the binding of Omicron SGP RBDs to heparin, with much less effects on WT or Delta. The pH dependence indicates different charged residues were present at the Omicron SGP-heparin interface. Detailed kinetic and structural analysis of the interactions of SARS-CoV-2 SGP RBDs with heparin provides important information for designing anti-SARS-CoV-2 molecules.

Interactions between heparin and SARS-CoV-2 spike glycoprotein RBD from omicron and other variants
https://www.frontiersin.org/articles/10.3389/fmolb.2022.912887/full

Please bear with me. This is cryptic, but is completely logical when you see the parts of this puzzle assembled. For, you see, the Spike Protein has a Prion Domain at its RBD.

They found a prion-like domain in the RBD of the SARS-COV-2 spike protein, which was missing from the original SARS-CoV virus. Asparagine (N) and glutamine (Q)-rich regions are characteristic features of many prion proteins.

A Potential Role of the Spike Protein in Neurodegenerative Diseases: A Narrative Review
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9922164/

Additionally, Heparin is important in the early nucleation stages of Prion Disease, promoting PrP aggregation.

We observed the whole aggregation process for full-length human recombinant PrP (23–231) aggregation on the heparin modified gold surface, from the formation of oligomers, to the assembly of protofibrils and short fibers, and the formation of elongated mature fibers. Heparin is found to promote the PrP aggregation by facilitating the formation of oligomers during the early nucleation stage.

Following the Aggregation of Human Prion Protein on Heparin Functionalized Gold Surface in Real Time
https://pubs.acs.org/doi/10.1021/acsabm.2c00779

Though this must be investigated further, there is an identifiable, clear path by which Heparin may become involved as a self-replicating Prionopathy. I will continue to pursue this hypothesis, and, of course, welcome the thoughts and contributions of all.

Thank you, as always, for your continued support, readership and dialog.