>https://zenodo.org/records/14559752
BREAKING: A NEW PRE-PRINT JUST DROPPED
The thrombo-inflammation and neuropathology sequence motifs of the SARS-CoV-2 spike protein appear to have been engineered into the virus
A landmark paper entitled, “Fibrin drives thrombo-inflammation and neuropathology in COVID-19,” was published in August 2024 that concluded the mechanism of the thrombotic and neurological symptoms following a SARS-CoV-2 infection, often called “long COVID,” is attributable to the binding of fibrin to discrete portions of the spike protein, specifically three N-terminal domains. This paper is a high impact publication with >110,000 views, placing it in the 99th percentile of articles published contemporaneously.
Here I examine the regions of the spike protein that bind to fibrin, fibrinogen, or both. The N-terminus of the spike protein contains the three strongest binding peptides and surprisingly, these regions are also the three insertions in the protein sequence that are unique to SARS-CoV-2 and not found in natural sarbecoviruses. All pre-pandemic sarbecoviruses have either a partial deletion in these regions or have protein amino acid substitutions that are non-conserved and therefore would not support fibrin binding.
This paper highlights an unusual set of facts:
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SARS-CoV-2 causes neuro-inflammation and its “long COVID” clinical findings through a mechanism whereby fibrin binds to the SARS-CoV-2 spike protein, forming proinflammatory blood clots.
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Three of the strongest binding motifs identified by Ryu et. al., are in the N-terminus of the SARS-CoV-2 Spike Protein.
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These motifs are contiguous to the three inserts identified in January 2020 that are not widely found in related-SARS viruses.
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These inserts are shown to have primary amino acid sequence homology to portions of the HIV gp120 protein that is responsible for CD4 cell receptor binding. While the sequences are individually small, making their probabilities of being randomly significant unlikely, when they are combined as a continuous 60-amino acid sequence, the homology to HIV is highly significant. The combination is justified because the non-contiguous sequences in HIV are none-the-less brought together to form the CD4 cell receptor binding protein.
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Antibodies from patients with HIV infections have been found which block the HIV CD4 recognition site and neutralize SARS-CoV-2. This demonstrates the three-dimensional homology of these regions in a functionally significant manner.
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A hypothesis that both HIV and SARS-CoV-2 can infect CD4 cells via this non-ACE2 interaction is supported by abundant clinical findings.
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HIV does not share the fibrin binding motifs seen in SARS-CoV-2 and, for the most part, evidence of direct HIV binding to fibrin has not been found.
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RaTG13 shares 59/60 amino acid homology and, for insert 3, a nt homology of 99.3%. Since there are numerous papers suggesting that RaTG13 has undergone laboratory genetic experiments, one much conclude that there is a likelihood that these unusual properties of SARS-CoV-2 did not arise naturally.