Intravenous Spike Protein Detoxification

Intravenous Spike Protein Detoxification
(PHOTOCREO Michal Bednarek/Shutterstock)
Dr. Peter A. McCullough
John Leake
3/4/2023
Updated:
5/15/2023

As COVID-19 vaccine victims are waking up to the reality that their bodies have been genetically loaded with either Pfizer or Moderna modifications (~70 percent homologous) of the Wuhan spike protein, a collective panic is driving a search for detoxification of this deadly protein proven to cause heart damage, neurological injury, blood clotting, and potentially more problems over the longer term.

Recently, vulnerabilities have been discovered in spike including proteolytic cleavage sites where the protein can be broken down by enzymes that could be suitable for drug development. In nature, there are many sources of such enzymes including worms.

The Japanese polychaete river worm Neanthes japonica (Izuka) is a known source of an alkaline serine protease abbreviated ASPNJ with the “N” for Neanthes japonica. Liu et al. have exploited the weaknesses found in spike and described them:

“The Spike protein of wild-type SARS-CoV-2 was 1273 aa in length [2,25], containing 103 K and R residues. The prediction using the ExPASy peptide cutter and our experimental results showed that 101 R and K sites could be hydrolyzed by trypsin and ASPNJ, except for 462KP (P, proline, pro) and 811KP (Supplement Table S1). The 11 K sites (including 417K) and 11 R sites in RBD of S1, as well as the 682R, 683R, and 685R in the CendR motif of S1 and the 825K, 835K, 847R, and 854K in the fusion peptide of S2, can all be hydrolyzed by ASPNJ.”

While Liu was targeting the wild-type spike protein of SARS-CoV-2, it is unknown whether the current Omicron strain or the altered Pfizer and Moderna versions of spike would have these same sites for hydrolysis.
Liu J, Kan M, Zhang L, Yue Y, Wang S, Hong M, Hong X. Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine Protease. Molecules. 2022 Mar 14;27(6):1882. doi: 10.3390/molecules27061882. PMID: 35335246; PMCID: PMC8954242.
Liu J, Kan M, Zhang L, Yue Y, Wang S, Hong M, Hong X. Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine Protease. Molecules. 2022 Mar 14;27(6):1882. doi: 10.3390/molecules27061882. PMID: 35335246; PMCID: PMC8954242.

APSNJ dissolved spike even at low concentrations within minutes and is believed to be viable for intravenous drug development. As these findings help propel the field forward, the next steps for Liu’s lab would be to repeat the experiments with the current Omicron strain, Pfizer, and Moderna spike protein families, and determine if there is equal dissolution.

While the public has been bashing “Big Pharma” for fraud and corruption in the COVID-19 vaccine debacle, there is a great need for the industry to step in and develop detoxifying agents or other methods to ameliorate spike protein damage to the human body from either vaccination or post-COVID-19 syndrome, and commonly in those with both exposures.

Reposted from Peter A. McCullough’s Substack
References:
Dr. McCullough is a practicing internist, cardiologist, and epidemiologist in Dallas, Texas. He studies the cardiovascular complications of both the viral infection and the injuries developed from COVID vaccines. He has dozens of peer-reviewed publications on COVID, multiple U.S. and state Senate testimonies, and has commented extensively on the medical response to the COVID crisis on major media outlets.
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