Q-01 · Open question
Does SARS-CoV-2 contain prion-like domains?
Investigating whether proteins of SARS-CoV-2 — particularly the spike protein — carry sequences or domains that could misfold and act as prions, or induce prion-like disease in humans.
Prion Investigation
Prion Research Investigation Project
A hard question, tested in the open.
Hypothesis“Have the COVID-19 virus and the subsequent implementation of coerced or mandated vaccines exposed the human population to potentially fatal prions?”
That is the question this project was set up to answer — a hypothesis, not a conclusion. The investigation addresses concerns raised in the scientific community about prion-like domains in SARS-CoV-2 proteins, and whether the vaccines developed in response to COVID-19 might have unforeseen long-term neurological effects. It runs in public: experiments streamed, methods disclosed, claims labeled by evidence level.
Research program
Four questions, one methodology.
Q-02 · Open question
Can infection or vaccination trigger prion formation?
Exploring whether natural infection with COVID-19, or exposure to spike proteins through mRNA vaccines, can lead to prion formation or neurodegeneration in human cells or animal models.
Q-03 · Open question
What are the mechanisms of potential prion formation?
Identifying the molecular mechanisms by which prion formation could occur in the context of infection or vaccination — the pathways of protein misfolding and aggregation.
Q-04 · Open question
What are the long-term implications for public health?
Assessing potential long-term neurological risks associated with COVID-19 and its vaccines — and what they would mean for vaccine safety, policy and pandemic preparedness.
Methods the project draws on
- In vitro
- Human and animal cell cultures — misfolding and aggregation assays
- Animal models
- Transgenic mice to study prion formation and neurodegeneration
- Biochemical assays
- PMCA and RT-QuIC to detect prion-like activity
- Structure analysis
- Computational modelling of protein folding and prion-like domains
Peer-reviewed basis Hypothesis PMCA and RT-QuIC are established assays in the prion literature; the in vitro, animal-model and computational arms are this project’s own investigative program, and their outcomes are not yet in.
Latest updates
Latest from the bench.
- NOV 28 2024 High Amyloidogenicity In Post Mortem
- NOV 21 2024 PrP^Sc Formation & Detection Lab Update
- NOV 22 2024 Has Prions Infected Humanity
- AUG 26 2024 Prion Research Investigation — Update
- AUG 17 2024 Prion Research Investigation Project Update
- AUG 11 2024 Prion Research Investigation — Update
Recorded live streams — raw updates as the investigation runs, not conclusions. The full video archive includes the SEM-EDX and Raman spectroscopy sessions.
Open lab · Funding
Audience-funded. Publicly accountable.
This investigation is 100% public funded — support from viewers keeps the experiments, the streams and this site running. Donations run through Stripe, the verified channel; where every yen goes is documented in the Open Lab ledger.
Investigation updates, as they happen
Protocol updates, methods notes and stream schedules. Written by the lab, not by an algorithm.
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