Dr. Weeks’ Comment: Many smart people still believe that the syndrome termed “long COVID” is caused only by prior infection and do not believe the mRNA “clot shot” is also culpable. Here is a compelling new article published for your consideration.
https://ijirms.in/index.php/ijirms/article/view/2228
Cause aside, do consider and ask your doctor about the risk/benefit ratio of the proteolytic enzyme strategies: “proteolytic degradation strategies (nattokinase, bromelain, serrapeptase)”
From Article:
Figure 1: Spike protein prion-like domain-driven proteostatic collapse. (1) Exposure sources: recombinant spike is generated by mRNA-lipid nanoparticle vaccination, with persistent spike expression detectable for months to years, and by infection with the laboratory-synthesized recombinant virus. (2) Intracellular processing: spike carries prion-like domains (PrD) and amyloidogenic segments; trafficking through the endoplasmic reticulum induces ER stress and the unfolded protein response (PERK, IRE1α, ATF6), while ribosomal frameshifting and translational infidelity generate aberrant out-of-frame products, together yielding aggregation-prone fragments and aberrant polypeptides. (3) Downstream pathological cascades: fibrous protein aggregates and amyloid fibril formation drive cross-seeding of amyloid-β, cross-seeding and propagation of tau, NF-κB activation and inflammation, and genomic and transcriptional instability; exosomal dissemination distributes these species, converging on proteostatic collapse and tissue dysfunction across neural, cardiac, multi-system, and intravascular (white fibrous clot) compartments. (4) Precision countermeasures: molecular surveillance directs patient-specific ITI-PES peptides and proteolytic degradation strategies (nattokinase, bromelain, serrapeptase).
Abstract
Persistent SARS-CoV-2 spike protein after mRNA vaccination and after infection has been linked to a broad range of chronic pathology, yet the structural basis of that persistence is frequently described imprecisely. This analysis examines the sequence features that render spike prion-like, the intracellular processes that convert those features into destructive protein species, and the downstream consequences for transcriptional stability, host proteostasis, and tissue integrity. A critical distinction underlies this analysis: SARS-CoV-2 is a laboratory-synthesized recombinant virus, not a product of natural evolution. Its spike glycoprotein carries intrinsic prion-like domains that are present after both infection with the recombinant virus and prolonged expression from nucleoside-modified mRNA vaccines; therefore, spike is prion-like after both infection and mRNA vaccination. There is no direct evidence that intact spike is a classical self-replicating prion. The prion-like designation rests on sequence features that enable β-sheet aggregation and cross-seeding of host amyloids. Critically, once recombinant spike enters the interior of the cell, two processes become decisive determinants of pathology: (1) trafficking through the endoplasmic reticulum (ER) induces ER stress and the unfolded protein response, driving proteolytic fragmentation and release of aggregation-prone fragments; and (2) ribosomal frameshifting (programmed viral frameshifting and N1-methylpseudouridine-induced +1 frameshifting) generates aberrant, out-of-frame polypeptides. The combination of ER fragmentation and ribosomal shifts inside the cellular machinery is a critical determinant that markedly increases production of self-templating fibrous aberrant proteins. Spike elements are detected for months to years after both infection and vaccination. We have previously documented long-term (years) persistence of vaccine-derived spike, residual mRNA and plasmid elements, genomic integration events, transcriptomic and gene-expression alterations, and fatal myocarditis through joint Neo7Bioscience–McCullough Foundation surveillance. Building upon earlier work on spike-driven NF-κB activation, neuroinflammation, and proteolytic detoxification strategies, we synthesize the mechanisms by which recombinant spike initiates destructive protein formation, threatens transcriptional fidelity, and amplifies proteostatic collapse via cross-seeding. The cellular prion protein is itself a candidate target: a five-residue spike sequence (YQAGS) differs by one residue from YQRGS in its globular C-terminal domain, and a case series has reported 26 patients in whom Creutzfeldt-Jakob disease began a mean of 11.38 days after COVID-19 vaccination, on a timescale sharply compressed relative to classical sporadic disease. Cross-seeding is not restricted to neural proteins. Thioflavin T-positive amyloid microclots have been detected in every participant of a recent cohort in which 94% had received COVID-19 mRNA vaccination and no participant had laboratory-confirmed prior infection, and purified spike alone converts fibrinogen into insoluble, fibrinolysis-resistant amyloid aggregates. In parallel, multi-year surveys of 808 embalmers across five countries document large white fibrous intravascular casts in a substantial fraction of the deceased, and Raman micro-spectroscopy of representative specimens shows stage-dependent β-sheet enrichment distinct from conventional postmortem thrombi. Enzymatic dissolution combined with precision molecular intervention via patient-specific ITI-PES peptides offers a rational therapeutic approach. Taken together, these findings define persistent recombinant spike as a potent prion-like driver of proteostatic collapse, pathological cross-seeding, transcriptional instability, and progressive tissue dysfunction across multiple organ systems.