Dr. Phlip McMillan,  John McMillan

Floating within the gut are microscopic saboteurs: misfolded proteins gone rogue that silently sneak into the brain, corrupting it’s intricate machinery. These prion proteins spark chain reactions, turning neighbouring molecules into malfunctioning “zombies” and wreaking havoc in the nervous system. They underlie conditions such as Creutzfeldt-Jakob disease (CJD), often mentioned alongside mad-cow disease. Physicians who have seen CJD never forget it; many simply call it “a nightmare.” Recent puzzling CJD cases in Oregon, together with reports of abnormal blood clots, are prompting a closer look at these enigmatic proteins and their possible links to COVID-19.

Understanding Prions: the “Zombie” Proteins

A prion is a normal body protein, commonly near nerve cells, that adopts a misfolded shape. The misfolded prion then induces other, normal versions to misfold in turn. Scientists liken this to one rotten strawberry spoiling an entire basket. The self-propagating corruption spreads, eventually riddling the brain with microscopic holes, creating a sponge-like texture and leading to catastrophic neurological failure. Related disorders include scrapie in sheep and kuru in humans, but CJD remains the most common human prion disease. Crucially, the normal prion protein PrPc is not harmful. It’s a standard component of our cells, particularly abundant on neurons where it’s involved in functions like synaptic transmission. Trouble arises only when it flips into the pathogenic PrPSc form. Whether that flip happens is influenced by genetics. A specific variation at codon 129 in the PRNP gene, which codes for the prion protein, determines whether a person carries methionine (M) or valine (V) at that position. Those with two copies of methionine – representing about 37% of Europeans but over 90% of East Asians – appear to be at the highest risk for sporadic CJD. This genetic factor underscores why prion disease risk isn’t uniform across the population. CJD appears in three main forms:

• Sporadic: seemingly random onset.
• Acquired: infection via contaminated instruments or, historically, by eating infected tissue.
• Familial: inherited genetic mutations.

Unlike Alzheimer’s disease, which unfolds over five to ten years, CJD can devastate a patient within weeks or months. That speed is its most recognisable clue. Dr. Philip McMillan, a clinician and researcher who has managed a patient with CJD, remarked based on a specific 2021 case, “The patient was independently well… On Sunday, she didn’t feel so well… By the following Tuesday [9 days later], she was semi-comatose… she died a little bit over a month after she was admitted,” noting that “the deterioration was like nothing I had ever seen before.”

Could COVID-19 Accelerate Prion Disease?

A July 2020 case report described a 60-year-old man whose first CJD symptoms appeared alongside COVID-19. The authors suggested that the virus’s intense inflammatory “cytokine storm” might have accelerated an underlying prion process. The patient’s decline was stark: developing fever, confusion, and forgetfulness shortly after a COVID diagnosis, progressing within weeks to speech difficulties, unsteady gait, and involuntary muscle jerks. This potential interaction is concerning, especially considering the virus’s unprecedented nature. Beyond systemic inflammation, some researchers are investigating a more direct molecular link involving the SARS-CoV-2 spike protein. While the intact SARS-CoV-2 spike does not behave like a prion, a buried stretch within it shows prion-like properties once the protein is clipped by enzymes such as neutrophil elastase. This degradation could potentially expose these embedded prion-like domains. Once exposed, these fragments could, in theory, interact with the body’s normal PrPc proteins, triggering misfolding and CJD-like pathology, or potentially interact with other proteins, such as fibrinogen in the bloodstream, contributing to the formation of unusual amyloid-like clots. The documented persistence of spike protein in various tissues, including the brain and its surrounding structures, adds weight to concerns over prolonged exposure. One case cannot prove a connection, but it raises an important question. In the United Kingdom, official CJD diagnoses have been falling. While this might seem positive, a counterintuitive possibility has been raised: perhaps the disease is now progressing so rapidly in some cases that individuals pass away before a full neurological workup and diagnosis can be completed. Whenever dementia evolves with unusual speed, clinicians should keep prion disease on the radar.

Prion-Like Proteins Found in Unusual Clots

Embalmers have reported rubbery, elongated blood clots since the COVID-19 pandemic began, phenomena initially dismissed by some but now subject to increasing scientific scrutiny. Researcher Kevin McCairn analysed several of these clots with Raman spectroscopy and RT-QuIC, a test that detects the “seeding” activity typical of prions. His preliminary results suggest the presence of amyloid protein structures – a hallmark of many neurodegenerative diseases – and, more strikingly, proteins exhibiting prion-like functional behavior. The RT-QuIC assay, specifically designed to detect the “seeding” activity characteristic of prions, reportedly showed results indicating high confidence for such activity in the clot samples. McCairn’s research posits a potential link between these clot characteristics and the spike protein of SARS-CoV-2, which could originate from infection or, controversially, from mRNA vaccination. Public health authorities stress that no credible evidence yet ties COVID-19 vaccines to neurodegenerative disease. McCairn’s results await independent verification, which is costly and technically demanding, but the observations raise significant questions. The implications of finding prion-like activity within these unusual clots extend beyond the brain. If spike protein fragments can indeed induce amyloid formation systemically, interacting with blood components like fibrinogen and potentially trapping other elements like hemoglobin and antibodies (as suggested by analysis of these clots), it could represent a novel systemic pathology, perhaps describable as a form of “systemic amyloid clotting.” This differs significantly from traditional CJD, which is primarily neurological, and raises concerns about widespread vascular and organ issues related to persistent, abnormal clot formation that resists normal breakdown processes.

Navigating Uncertainty: Why Rigorous Investigation Matters

The intersection of long-known prion biology, COVID-19 inflammation, spike-protein fragments and amyloid-rich clots sketches a complex, unsettling landscape. Prion diseases are currently untreatable once symptoms emerge. If prion-like protein structures are indeed forming systemically, as McCairn’s research and related hypotheses suggest, the implications could be far-reaching. Confronting these possibilities should be framed not as fearmongering, but as due diligence. “Risk mitigation means that you have to consider the worst outcomes,” Dr. McMillan states, adding a stark warning: “We must stop thinking of CJD as rare and random. In a world of persistent spike proteins, prion disease may no longer be a distant threat but an urgent signal.” The next step is urgent, independent research. Key questions include:

1. Mechanism – Are inflammation or spike fragments genuinely driving prion misfolding, or merely hastening an existing process?
2. Surveillance – Should RT-QuIC testing extend to unexplained rapid dementias and to these atypical clots?
3. Replication – Will larger, blinded studies confirm McCairn’s findings?
4. Genetics – Does codon 129 genotyping help identify those at greatest risk?

Causation is unproven, but the possibility warrants serious scrutiny. Ignoring early, even uncomfortable, signals could delay vital discoveries, and leave us unprepared for threats we might yet prevent.