Page 23 - Dr Stephanie Seneff - Reviewing Some Possible Unintended Consequences of the mRNA Vaccines Against COVID - 19

amyotrophic lateral sclerosis (ALS) may be prion diseases, and researchers have identified specific
proteinaceous infectious particles linked to these diseases (Weickenmeier et al., 2019).

Furthermore, researchers have identified a signature motif linked to susceptibility to misfolding into
toxic oligomers, called the glycine zipper motif. It is characterized by a pattern of two glycine
residues spaced by three intervening amino acids, represented as GxxxG. The bovine prion linked to
MADCOW has a spectacular sequence of ten GxxxGs in a row (see uniprot.org/uniprot/P10279).

More generally, the GxxxG motif is a common feature of transmembrane proteins, and the glycines
play an essential role in cross-linking α-helices in the protein (Mueller et al., 2014). Prion proteins
become toxic when the α-helices misfold as β-sheets, and the protein is then impaired in its ability to
enter the membrane (Prusiner, 1982). Glycines within the glycine zipper transmembrane motifs in
the amyloid-β precursor protein (APP) play a central role in the misfolding of amyloid- β linked to
Alzheimer’s disease (Decock et al., 2016). APP contains a total of four GxxxG motifs.

When considering that the SARS-CoV-2 spike protein is a transmembrane protein, and that it
contains five GxxxG motifs in its sequence (see uniprot.org/uniprot/P0DTC2), it becomes
extremely plausible that it could behave as a prion. One of the GxxxG sequences is present within
its membrane fusion domain. Recall that the mRNA vaccines are designed with an altered sequence
that replaces two adjacent amino acids in the fusion domain with a pair of prolines. This is done
intentionally in order to force the protein to remain in its open state and make it harder for it to fuse
with the membrane. This seems to us like a dangerous step towards misfolding potentially leading to
prion disease.
A paper published by J. Bart Classen (2021) proposed that the spike protein in the mRNA vaccines
could cause prion-like diseases, in part through its ability to bind to many known proteins and
induce their misfolding into potential prions. Idrees and Kumar (2021) have proposed that the spike
protein’s S1 component is prone to act as a functional amyloid and form toxic aggregates. These
authors wrote that S1 has the ability “to form amyloid and toxic aggregates that can act as seeds to
aggregate many of the misfolded brain proteins and can ultimately lead to neurodegeneration.”

According to Tetz and Tetz (2020), the form of the spike protein in SARS-CoV-2 has prion regions
that are not present in the spike proteins for other coronaviruses. While this was reported in a non-
peer-reviewed article, the authors had published a previous paper in 2018 identifying prion-like
regions in multiple eukaryotic viruses, so they have considerable expertise in this area (Tetz and
Tetz, 2018).

A final point here relates to information about the Pfizer vaccine in particular. The European
Medicines Agency (EMA) Public Assessment Report is a document submitted to gain approval to
market the vaccine in Europe. It describes in detail a review of the manufacturing process as well as
a wide range of associated testing data. One concerning revelation is the presence of “fragmented
species” of RNA in the injection solution. These are RNA fragments resulting from early
termination of the process of transcription from the DNA template. These fragments, if translated
by the cell following injection, would generate incomplete spike proteins, again resulting in altered
and unpredictable three-dimensional structure and a physiological impact that is at best neutral and
at worst detrimental to cellular functioning. There were considerably more of these fragmented

International Journal of Vaccine Theory, Practice, and Research 2(1), May 10, 2021 Page | 411