GET READY FAGGOTS, BECAUSE WE'RE GOING DOWN THE FUCKING RABBIT HOLE

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4903029/

>Specifically, use of these building blocks to investigate protein folding and misfolding has been of particular value since it can provide tremendous insights into peptide aggregation related to a variety of protein misfolding diseases, or amyloid diseases (e.g. Alzheimer’s disease, Parkinson’s disease, type-II diabetes). Herein, the self-assembly of TK9, a 9 residue peptide of the extra membrane C-terminal tail of the SARS Corona virus envelope, and its variants were characterized through biophysical, spectroscopic and simulated studies, and it was confirmed that the structure of these peptides influence their aggregation propensity, hence, mimicking amyloid proteins.

>It has been found that amyloid-related diseases (e.g., Alzheimer’s disease (AD), Prion diseases, Type II diabetes, Parkinson’s disease, and Huntington’s disease) are connected by the aggregation of relatively unstructured monomers into a β-sheet rich fibrillar aggregates.
So first off we've established that one major detail, that is the very STRONG similarities between SARS and prion diseases, along with several others. The two things all they share in common has to do with amyloid proteins, and their role in the brain itself. Perhaps you might be wondering how type II diabetes could possibly fit in, I assume most people aren't aware of the neurological component.

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5411686/
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5623586/
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2797942/
> Although the mechanism responsible for β-cell dysfunction and death is not completely understood, recent findings suggest that the accumulation of misfolded aggregates of the islet amyloid polypeptide (IAPP) in the islets of Langerhans may play an important role in pancreatic damage. Misfolding and aggregation of diverse proteins and their accumulation as amyloid in different organs is the hallmark feature in a group of chronic, degenerative diseases termed protein misfolding disorders (PMDs).
>Patients with diabetes have been found to have several changes in brain structure that appear to develop over time and often experience conditions that present risk for subsequent cognitive dysfunction. Future study is necessary to define the natural history, structural basis, and risk factors for cognitive dysfunction in diabetes.
>Adults with diabetes have also been found to have structural changes, including atrophy and leukoariosis.
The mode of action inside the brain isn't quite as clear cut, as these have been shown in treated diabetes as well. It fits in as a much milder form of the others on that list.

Okay so we've taken the time to establish the important point here, that is the connection between prion diseases, and others. The main connections being as stated above amyloid proteins and brain involvement. So back to SARS!

https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0064013
>Severe acute respiratory syndrome coronavirus (SARS-CoV) membrane (M) proteins are capable of self-assembly and release in the form of membrane-enveloped vesicles, and of forming virus-like particles (VLPs) when coexpressed with SARS-CoV nucleocapsid (N) protein. According to previous deletion analyses, M self-assembly involves multiple M sequence regions.

>Ratios of M levels in medium to those in cells were determined for each mutant and normalized to wt medium/cell ratios in parallel experiments. Error bars indicate standard deviations. *, p<0.05; **, p<0.01. (B) A FLAG tagged at the M carboxyl terminus prevents VLP assembly. 293T cells were transfect with SARS-CoV N alone or together with the indicated wt or mutant M expression vector. At 24 to 36 h post-transfection, supernatants and cells were collected and prepared for protein analysis as described above. (C–D) Results from cross-linking analyses of SARS-CoV M and HIV-1 Gag proteins.

Significance?

https://www.fasebj.org/doi/full/10.1096/fj.01-0442hyp
>Despite its fundamental clinical importance, the mechanism of amyloid formation is not fully understood. When we analyzed a variety of short functional fragments from unrelated amyloid-forming proteins, a remarkable occurrence of aromatic residues was observed. The finding of aromatic residues in diverse fragments raises the possibility that π-π interactions may play a significant role in the molecular recognition and self-assembly processes that lead to amyloid formation.

https://www.ncbi.nlm.nih.gov/pubmed/9234739
>This protein has two homologs, Wtm2p and Wtm3p, which probably arose by gene duplications. Deletion of these genes affects transcriptional repression at several loci, including derepression of IME2, a meiotic gene normally repressed in haploid cells. Targeting of these proteins to DNA resulted in a dramatic repression of activated transcription. In common with a mutation in the histone deacetylase RPD3, wtm mutants showed increased repression at the silent mating-type locus, HMR, and at telomeres. Although all three Wtm proteins could act as transcriptional repressors, Wtm3p, which is the least homologous, appeared to have functions separate from those of the other two.

Okay so tell you something you don't already know, right? We're establishing the data that's important to what comes next.

https://www.sciencedirect.com/topics/veterinary-science-and-veterinary-medicine/chronic-wasting-disease
>Amyloidosis is a chronic wasting disease of animals caused by the tissue deposition of fibrils formed by the polymerization of protein subunits arranged in a specific beta-pleated sheet biochemical conformation.48 Reactive systemic amyloidosis may occur as a sequela to chronic inflammatory or neoplastic disease, although in some instances no predisposing cause is identified.
Sound familiar?

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3457318/
>Furthermore, it has been shown that RNA molecules facilitate in vitro amplification of infectious PrPSc (9, 15, 33). However, the exact role of RNA in the amplification process remains unknown. RNA could act as a mere catalyst of the PrP misfolding process.

>In the present study, we further investigated the possibility of a strain-specific dependency upon RNA during in vitro PrPSc amplification and addressed the role of RNA as a strain-specifying component of infectious prions. For this purpose, we conducted PMCA amplification of various mouse prions in RNA-depleted as well as control reaction mixtures. We studied the role of RNA in the efficiency of the amplification reaction for each of 9 strains of mouse prions. We determined RML strain characteristics by bioassay after amplification in RNA-depleted versus control PMCA reactions. We conclude that RNA dependency for in vitro conversion is prion strain specific and that RML prion strain identity is maintained after in vitro amplification under conditions of RNA depletion. We propose that RNA molecules may act as strain-specific catalysts of prion replication.
This is HIGHLY significant for the main point of this.

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5997743/
>Prions are proteins that can self-propagate, leading to the misfolding of proteins. In addition to the previously demonstrated pathogenic roles of prions during the development of different mammalian diseases, including neurodegenerative diseases, they have recently been shown to represent an important functional component in many prokaryotic and eukaryotic organisms and bacteriophages, confirming the previously unexplored important regulatory and functional roles. However, an in-depth analysis of these domains in eukaryotic viruses has not been performed. Here, we examined the presence of prion-like proteins in eukaryotic viruses that play a primary role in different ecosystems and that are associated with emerging diseases in humans.

The similarities between SARS and prion diseases is far more than you would ever imagine, prion-like domain of SARS is very bad for us when you consider chronic wasting-disease.

So let's say SARS-CoV-2 jumps to the deer population, and starts infecting deer already infected with chronic wasting-disease. We're in a VERY dangerous possible situation here.