A paper published in Nature Communications last week set out to understand the molecular mechanisms which cause neurological symptoms reported “in up to 30% of [Covid] cases.” Neurological symptoms such as memory loss, sensory confusion, severe headaches, and even stroke are thought to be produced by the virus infecting the central nervous system.
“The neurological effects of Covid-19 share similarities to neurodegenerative diseases in which the presence of cytotoxic aggregated amyloid protein or peptides is a common feature … We suggest that cytotoxic aggregates of SARS-CoV-2 proteins may trigger neurological symptoms in Covid-19.” the study authors wrote.
“This [study] is about the Open Reading Frames (ORFs) and NOT the spike protein,” Jessica Rose wrote in an article explaining the findings of the study, see below. However, she asks: are amyloidogenic peptides residing in the SARS-nCoV-2 spike protein and since the modified spike proteins, used in the Moderna and Pfizer injectable biological products, are derived from the SARS-nCoV-2 spike, do these proposed amyloidogenic properties carry over?
Set aside your beliefs about whether a “virus” by your definition exists or not and think about the implications. The key to understanding the significance of this study’s findings is to understand what amyloids are.
Amyloids are aggregates of proteins and the word “amyloidogenic” means producing or tending to produce amyloid deposits. A 2014 article titled ‘When amyloids become prions’ noted all amyloids could be considered prions – from those involved in cell-to-cell transmission to those responsible for real neuronal invasion. A 2008 article titled ‘Amyloid fibrils’, aiming to highlight the key scientific findings and discuss how the stability of amyloid fibrils impacts bionanotechnology, concluded:
“Amyloid refers to the abnormal fibrous, extracellular, proteinaceous deposits found in organs and tissues … Amyloid fibrils are extremely strong, highly ordered and organised fibres that can be formed by a large number of proteins and peptides. Their stability and insolubility mean that they are useful in a large number of naturally occurring forms as well as bionanotechnology. However, it also means that they are destructive and have the ability to accumulate in the tissues in disease.”
Amyloid fibrils, Prion, 25 November 2008
We wonder if amyloidogenic peptide “vaccines” could provide insight into the extraordinary fibrous “clots” or biostructures being found by embalmers post-Covid injection, as being investigated by Dr. Jane Ruby and Mike Adams, see HERE and HERE. Could it be related? We don’t know and will have to wait and see what evidence further investigation provides.
Further reading: Bacteria’s amyloids display surprising structure, Science News, 23 February 2017
Below is Jessica Rose’s article, ‘An incredible paper was just published’ explaining the findings of the paper published last week in Nature Communications.
By Jessica Rose
Please read this paper entitled: “Neurotoxic amyloidogenic peptides in the proteome of SARS-COV2: potential implications for neurological symptoms in Covid-19”. It was published in Nature Communications on June 13, 2022.1
The bottom line of this incredible work is that there are two amyloidogenic proteins for in the Open Reading Frames (ORF) 6 and 10 from SARS-nCoV-2 (the ORF-10 one does not have a homologue in SARS-nCoV – that means it’s unique to SARS-nCoV-2), that form crystalline amyloid structures independently, and together, at room temperature!, very quickly, and that these structures induce programmed cell death in neural cells.
Before I unpack this article, I want to say something. I think this was able to be published in this prestigious journal for 2 reasons:
- this is about Covid-19 (SARS-nCoV-2) and
- this is about the ORFs and NOT the spike protein amyloidogenic peptides.
Let’s start. These amazing people did the same kind of thing as described in this paper that I described HERE. To briefly summarise, they used amyloid prediction algorithms (TANGO) and other bioinformatics tools (ZIPPER) to provide choices of residue windows of specific lengths. They found 2 contender amyloidogenic peptides that reside in the SARS-nCoV-2 ORFs 6 and 10: ILLIIM and RNYIAQVD, respectively. These were the two that they decided to synthesise and study because of their predicted amyloidogeneticity potential.
Amyloid aggregation prediction algorithms identified two short peptides from ORF6 and ORF10 that are likely to form amyloids.
My readers know all too well by now (because you’re amazing), that amyloid proteins are really beta-sheet rich. Below is Figure 1 from the paper which shows where the peptides reside in the respective ORFs (ORF-6 and ORF-10) and their beta sheet propensities.
Nanoscale imaging reveals both peptide sequences self-assemble into polymorphic amyloid assemblies.
Two things struck me about the conditions under which the structures assembled: assembly happened at room temperature and it happened immediately.
Atomic force microscopy (AFM) imaging of the two peptide assemblies revealed that both peptides assembled at 37 °C almost immediately at 1 mg mL−1 (Supplementary Figs. 1 and 2) into a highly polymorphic mixture of nanofibrous and crystalline structures.
Aren’t those images incredible! The needle-like structures that each peptide formed independently were slightly different whereby:
ILLIIM tends to form very large (2–3 μm in width) multi-laminar crystalline assemblies (Fig. 2g), whereas RNYIAQVD predominantly forms long linear needle-like structures.
Another thing that struck me about what they found was these peptides that assemble into these structures “tend[ed] to stack on top of each other forming multi-laminar structures.”
The authors used all sorts of techniques such as “X-ray scattering, spectroscopic characterisation, fluorescent microscopy and molecular modelling to confirm the amyloid nature of the assemblies.”
In light of these incredible findings, there still may not be an effect in vivo or the living organisms like humans. They hypothesised toxicity to human neurons and investigated this hypothesis using a human cell line called SH-SY5Y exposed to both ILLIIM and RNYIAQVD. They found that ILLIIM and RNYIAQVD triggered late-stage apoptosis in the cells (programmed cell death) whereas ILLIIM did so prominently as very low concentrations (0.04 mg mL−1 vs 0.15 mg mL−1 for ILLIIM and RNYIAQVD, respectively.
Summary: Two peptides from ORF-6 and ORF-10 of SARS-nCoV-2 induce apoptosis in human neural cells.
They subsequently conclude that this is what’s causing all the neurological problems associated with Covid-19.
The cytotoxicity and protease-resistant structure of these assemblies may result in their persistent presence in the CNS of patients post-infection which could partially explain the lasting neurological symptoms of Covid-19.
I know what you’re thinking.
Let’s ask the three questions of our lifetimes, shall we?
Question 1: Are amyloidogenic peptides residing in the SARS-nCoV-2 spike protein and are they capable of inducing apoptosis in neural cells and/or other cell types?
Question 2: Since the modified spike proteins, used to construct the LNP-encased payload in the Moderna and Pfizer injectable biological products, are derived from the SARS-nCoV-2 spike, do these proposed amyloidogenic properties carry over?
Question 3: If the modified spike protein in the Covid-19 injectable products contains amyloidogenic peptides capable of assembling into amyloid structures, is this why we are seeing such systemic neurological, hepatological, cardiovascular and reproductive damages with regard to adverse event reports in databases such as VAERS, Eudra and Yellowcard?
- 1 Charnley, M., Islam, S., Bindra, G.K. et al. Neurotoxic amyloidogenic peptides in the proteome of SARS-COV2: potential implications for neurological symptoms in Covid-19. Nat Commun 13, 3387 (2022). https://doi.org/10.1038/s41467-022-30932-1.
- 2 Baric Ralph A. et al., Severe Acute Respiratory Syndrome Coronavirus Open Reading Frame (ORF) 3b, ORF 6, and Nucleocapsid Proteins Function as Interferon Antagonists. Journal of Virology. 2007. Vol. 81, No.2 https://journals.asm.org/doi/10.1128/jvi.01782-06?permanently=true.
- 3 Lei, X., Dong, X., Ma, R. et al. Activation and evasion of type I interferon responses by SARS-CoV-2. Nat Commun 11, 3810 (2020). https://doi.org/10.1038/s41467-020-17665-9.
- 4 Lee, JG., Huang, W., Lee, H. et al. Characterization of SARS-CoV-2 proteins reveals Orf6 pathogenicity, subcellular localization, host interactions and attenuation by Selinexor. Cell Biosci 11, 58 (2021). https://doi.org/10.1186/s13578-021-00568-7.