Unraveling the Mystery of “Embalmer Clots”: A New Coagulopathy Linked to SARS-CoV-2 and mRNA Vaccines ?

Disclaimer: This post is for informational purposes only and not medical advice. Always consult a qualified healthcare professional for medical concerns.

Embalmers have reported unusual, rubbery white clots obstructing arteries and veins in deceased individuals, particularly those with SARS-CoV-2 exposure and/or mRNA vaccination. Unlike typical red thrombi, these “embalmer clots” are resistant to fibrinolysis, rich in amyloid, and fluoresce under Thioflavin T staining, indicating a novel pathology. Ongoing research, integrating whole-genome sequencing (WGS), proteomics, and studies on modified nucleotides, suggests a new coagulopathy: Systemic Fibrinaloid Amyloid Coagulopathy (SFAC). This post examines the potential three-stage progression of these clots, their possible triggers, including modified nucleotides in mRNA vaccines, and the urgent need for further investigation. A video (Hirshman 2024) demonstrating the removal of a white clot is referenced here:

A Three-Stage Progression of Amyloid Clots

Blood clotting is your body’s way of stopping bleeding when you get a cut or injury, where tiny cells called platelets stick together at the wound to form a plug, and special blood proteins create a fibrin net to strengthen it into a solid clot that seals the leak until the injury heals. Recently, embalmers and some doctors have reported seeing unusual white, rubbery clots in deceased individuals, particularly since 2021, made mostly of fibrin and platelets with fewer red blood cells, unlike typical red clots. Embalmers say these clots, which resemble arterial or postmortem clots, appear in many cases, a frequency they find new or striking compared to before. (Haviland 2022-2024) Some suggest these could stem from changes in blood or clotting tendencies, possibly tied to inflammation or other recent physiological shifts, sparking discussion about underlying causes as observations continue.

Blood clotting (hemostasis) is typically described in three stages: vascular spasm, platelet plug formation, and coagulation, which form a stable clot to stop bleeding. Some models include clot retraction and fibrinolysis, expanding to four or five stages. Similarly, the progression of amyloid clots, evolving from conventional red clots to rigid, amyloid-rich white clots, may follow a distinct three-stage process influenced by genetic, environmental, and structural factors.

Stage I: Red Clots-The Foundation

Red clots, the body’s natural response to injury, comprise fibrin meshes, red blood cells, platelets, and hemoglobin. In individuals with SARS-CoV-2 exposure or mRNA vaccination, genetic predispositions may heighten clotting risks. Whole-genome sequencing has identified mutations that may promote abnormal clot formation:

• F5 mutations: Similar to Factor V Leiden, these increase clotting risk by enhancing thrombin generation. (Williamson 1998)

• F13B variations: Strengthen fibrin crosslinking, making clots more stable. (Xu 2022)

• GP1BA mutations: Disrupt platelet binding to von Willebrand factor, potentially altering normal coagulation. (Xu 2022)

A study by Pretorius et al. (2021) found that Long COVID/Post-Acute Sequelae of COVID-19 (PASC) patients exhibit persistent plasma micro-clots resistant to fibrinolysis, with elevated levels of α(2)-antiplasmin and inflammatory molecules like Serum Amyloid A (SAA). This suggests that hypercoagulation and impaired fibrinolysis are central to COVID-19-related pathologies, potentially laying the groundwork for further clot evolution.

Stage II: Transitional Clots-Amyloid Seeds Emerge

As clots evolve, amyloid formation may accelerate, transforming them into transitional structures. This stage may be driven by:

• Neutrophil Extracellular Traps (NETs): Activated by complement system dysregulation (e.g., MASP1 variants), NETs saturate the clot matrix, promoting inflammation and amyloidogenesis. (Zhou 2022, Borissoff 2011, Xu 2022)

• LRP1 Mutations: Frameshift-like mutations in LRP1 (Low-Density Lipoprotein Receptor-Related Protein 1) may impair amyloid-beta clearance, potentially contributing to amyloid accumulation. (Van Gool 2019) Speculatively, LRP1 dysfunction could also hinder clearance of lipid nanoparticles (LNPs) or spike proteins from mRNA vaccines, possibly exacerbating inflammation.

• Modified Nucleotides: N1-methyl-pseudouridine (m1Ψ) in mRNA vaccines may induce ribosomal frameshifting, producing misfolded proteins that may potentially seed amyloid formation (Mulroney 2023, Santiago 2022, 2023, 2024). This hypothesis is supported with by the fluorescence of transitional clots under Congo Red staining, a marker of amyloid deposition. (Pretorius 2021, GDR, 2024)

Stage III: White Clots, Is it a new type of fibrinoid?

Fibrinoid is a substance that resembles fibrin, a protein involved in blood clotting. In medical texts, fibrinoid necrosis describes a type of tissue damage that occurs in blood vessels, often due to immune reactions. High-performance liquid chromatography (HPLC) analysis reveals elevated fibrinogen-β and -γ chains in these clots, (see figure 1) alongside increased actin but an absence of thrombin, suggesting an unconventional clotting mechanism (GBDR, 2024).

Fig1- GBDR 2024, GDR 2024

Mature white clots exhibit a dense, rubbery texture, are heavily amyloid-packed, and fluoresce under Thioflavin T staining, though they lack the crystalline birefringence typical of some amyloids. (GDR 2024, McCairn 2025, Hirschman video 2024, Pretorius 2021, Nystrom 2022)

Elemental analysis：

Inductively coupled plasma mass spectrometry (ICP-MS) reveals:

· Phosphorus: 4,500 ppm (GBDR 2024, GDR 2024)

· Elevated tin and sulfur levels (GBDR 2024)

These findings indicate a unique biochemical composition.

Amino Acid Composition

The amino acid composition (see fig 2) supports the formation of rigid, amyloid-rich structures:

· Proline (21.26%)

· Aspartic acid (16.3%)

· Lysine (16.2%)

· Minimal cysteine (0.137%)

High levels proline, aspartic acid, and lysine may influence to β-sheet aggregation in amyloid-rich clots, though further validation is needed to determine their precise role in fibrin-amyloid interactions. (GBDR 2024)

Fig 2-GBDR 2024, GDR 2024

Proline and Its Role in Clot Formation

Proline contributes to the structural integrity of clotting proteins, including fibrinogen, which serves as the precursor to fibrin in blood clot formation. While proline is not a direct clotting factor, its presence in clot-associated proteins plays a role in protein folding and stability. However, fibrin stability is primarily governed by cross-linking mechanisms rather than proline residues. Additionally, glutamine, along with glycine and alanine, occurs at higher concentrations in plasma and clotting proteins.(plasma amino acids)

Within clot-forming proteins like fibrinogen and collagen, proline plays a supportive role but is not uniquely abundant compared to other amino acids. In fibrinogen, glycine and aspartic acid are more prevalent than proline, while collagen is notably enriched with glycine and hydroxyproline.(https://kpfu.ru/staff_files/F430526914/Subcellular_Biochemistry_2017___Review.pdf)

Phosphate and Amyloid Formation

Phosphates are critical in amyloid protein formation, influencing phosphorylation, aggregation, and structural stabilization. Amyloid proteins, such as amyloid-beta (Aβ) in Alzheimer’s disease and alpha-synuclein in Parkinson’s disease, form insoluble fibrils that contribute to neurodegenerative disorders. Phosphorylation of Aβ peptides increases their aggregation propensity, with phosphate groups promoting β-sheet formation. Similarly, in vitro studies show that hyperphosphorylation of tau accelerates fibril assembly, reinforcing the link between phosphate interactions and pathological amyloid formation. (Simic 2016, Lövestam 2025)

Supporting Evidence: Amyloid Clots in Clinical and Forensic Studies

Recent studies provide compelling evidence for amyloidogenic clots:

-A 2024 medRxiv preprint by Grixti et al. (DOI: 10.1101/2024.11.01.24316555) found that clots retrieved from ischemic stroke patients via mechanical thrombectomy exhibit strong Thioflavin T staining, indicating a pervasive amyloid component and resistance to fibrinolysis, even in patients treated with thrombolytics. These findings, observed in a controlled clinical setting, parallel the amyloid-rich, fibrinolysis-resistant white clots reported by embalmers, suggesting that amyloidogenic clotting may be a broader phenomenon warranting further investigation into its triggers, such as SARS-CoV-2 and/or modified mRNA. (Grixti 2024)

-McCairn et al. (2025) reported in a Substack post that forensic analysis of cadaveric samples revealed rubbery, fibrin-like aggregates with beta-sheet-rich domains and dense fibrillar ultrastructure, also fluorescing under Thioflavin T staining. Preliminary PCR detected trace recombinant spike protein markers (e.g., SV40, Ori), suggesting a potential link to SARS-CoV-2 or vaccines, though these findings require peer-reviewed validation. (McCairn 2025)

These observations align with Pretorius et al. (2021), which identified amyloid micro-clots in Long COVID patients, suggesting that amyloidogenic clotting may be a broader phenomenon linked to COVID-19 pathology.

Modified Nucleotides: A Potential Trigger?

Research on modified nucleotides, particularly N1-methyl-pseudouridine (m1Ψ) in mRNA vaccines, suggests a possible link to SFAC. (Santiago 2022, 2023, 2024) While m1Ψ enhances mRNA stability, it may also introduce unintended effects:

• Ribosomal Frameshifting: Mulroney et al. (2023) found that m1Ψ can cause translational errors, potentially producing misfolded spike protein and fragments (e.g., sequences 192–211, Nystrom 2022) that may seed amyloid formation. (Mulroney 2023, Santiago 2022, 2023, 2024)

• Amyloidogenic Peptides: These aberrant proteins may form β-sheet-rich aggregates, resembling the amino acid profile of reported fibrous clots. (Nyström 2022, GBDR 2024).

• Vaccine Lot Variability: Schmeling et al. (2023) analyzed adverse events after BNT162b2 vaccination in Denmark (December 2020–January 2022), finding that 4.22% of batches, mainly smaller early lots, were linked to 70.78% of suspected adverse events, 27.49% of serious events, and 47.15% of event-related deaths. While this suggests batch-related differences, causation is unclear due to potential biases and population factors. Impurities in modified nucleotides might worsen frameshifting, potentially increasing SFAC risk in susceptible individuals.(Mulroney 2023, Schmeling 2023, Santiago 2022, 2023, 2024)

SFAC Formation

SFAC may arise from key factors:

1. Genetic Priming: Mutations in clotting genes (e.g.: F5, CPB2), amyloid-associated genes (e.g.: PSEN2, LRP1), and structural proteins (e.g.: SERPINB5, BIN1) may create a predisposition.

2. Environmental Triggers: Exposure to the SARS-CoV-2 spike protein , NET influx, and modified mRNA proteins may initiate amyloid seeding. (Pretorius 2021, Mulroney 2023, Santiago 2022, 2023, 2024)

SFAC is characterized by fibrin-amyloid cross-seeding, fibrinolysis resistance, a NET-rich matrix, and prionoid features like self-propagating beta-sheet structures.

Why This Matters: Broader Health Implications

· Potential Long-Term Risks of m1Ψ
N1-methylpseudouridine (m1Ψ) is a key modification in COVID-19 mRNA vaccines, such as BNT162b2, designed to improve mRNA stability and reduce immune activation. However, recent findings raise concerns:

· m1Ψ dampens innate immune responses by impairing RIG-I and toll-like receptor signaling, potentially affecting Type I interferon production.

· A 2024 study in the International Journal of Biological Macromolecules suggests that m1Ψ may stimulate cancer growth and metastasis, as observed in melanoma mouse models. (Rubio-Casillas 2024)

· "Evidence is provided that adding 100% N1-methyl-pseudouridine (m1Ψ) to the mRNA vaccine in a melanoma model stimulated cancer growth and metastasis, while non-modified mRNA vaccines induced opposite results, thus suggesting that COVID-19 mRNA vaccines could aid cancer development." (Rubio-Casillas 2024)

These findings underscore the need for further research and safety considerations. Modified nucleotides may inadvertently fuel amyloidogenic clotting processes, warranting continued investigation. (Mulroney 2023, GBDR 2024, GDR 2024, Santiago 2022, 2023, 2024)

A Call for Action

Some embalmers report observing white, fibrous clots in 20–30% of bodies since 2021, suggesting a potential health concern, though these findings are not confirmed by peer-reviewed autopsy studies. SFAC, a proposed coagulopathy, may contribute to long COVID symptoms, as by evidenced amyloid micro-clots, but links to vaccine injuries or sudden deaths require further research and investigation. (Pretorius 2021, Haviland 2024)

Urgent Action Needed on Potential SFAC Risks

The hypothesized link between modified nucleotides in mRNA vaccines and systemic fibrin amyloid micro-clots (SFAC) warrants immediate action:

• Regulatory Agencies: Intensify scrutiny of modified nucleotides, such as N1-methyl-pseudouridine, in mRNA vaccines to ensure batch consistency and safety (Schmeling, 2023; Santiago, 2022–2024).

• Healthcare Providers: Push for diagnostic codes to identify SFAC and adopt tools like Thioflavin T staining to detect amyloid in patients with unexplained clotting disorders. Report observations of unusual clots, such as those depicted in Hirshman’s (2024) video of white clot removal and the following video:

Join the Investigation

We are actively investigating clots and studying the effects of modified nucleotides. Have you observed these clots? Share your experiences below, let’s work together to unravel this mystery.

Disclaimer: This post is for informational purposes only and not medical advice. Always consult a qualified healthcare professional for medical concerns.

References

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GBDR 2024, GDR 2024. Amyloidogenic White Clots. Unpublished dataset (HPLC, ICP-MS, amino acid analysis).

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