CoVid mRNA vaccine and the risk of Prion disease (Study)


Prion diseases or transmissible spongiform encephalopathies (TSEs) are a family of rare progressive neurodegenerative disorders that affect both humans and animals. They are distinguished by long incubation periods, characteristic spongiform changes associated with neuronal loss, and a failure to induce inflammatory response.

The causative agents of TSEs are believed to be prions. The term “prions” refers to abnormal, pathogenic agents that are transmissible and are able to induce abnormal folding of specific normal cellular proteins called prion proteins that are found most abundantly in the brain. The functions of these normal prion proteins are still not completely understood. The abnormal folding of the prion proteins leads to brain damage and the characteristic signs and symptoms of the disease. Prion diseases are usually rapidly progressive and always fatal.

👉 Prion Diseases | CDC

© 2021 Classen JB. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License 

Research Article ISSN 2639-9458 • Microbiology & Infectious Diseases


Resources:

  1. Classen JB, Classen DC. Clustering of cases of insulin dependent diabetes (IDDM) occurring three years after Hemophilus influenza B (HiB) immunization support causal relationship between immunization and IDDM. Autoimmunity. 2002; 35: 247-253. 
  2. King OD, Gitler AD, Shorter J. The tip of the iceberg: RNA- binding proteins with prion-like domains in neurodegenerative disease. Brain Res. 2012; 1462: 61-80. 
  3. WHO, International Non Proprietary Names Program: 11889. 9/2020. 
  4. Kapeli K, Pratt GA, Vu AQ, et al. Distinct and shared functions of ALS-associated proteins TDP-43, FUS and TAF15 revealed by multisystem analyses. Nature Communications. 2016; 7: 12143. 
  5. Kuo P, Chiang C, Wang Y, et al. The crystal structure of TDP- 43 RRM1-DNA complex reveals the specific recognition for UG- and TG-rich nucleic acids. Nucleic Acids Research. 2014; 42: 4712-4722. 
  6. Tollervey JR, Curk T, Rogelj B, et al. Characterizing the RNA targets and position-dependent splicing regulation by TDP-43; implications for neurodegenerative diseases. Nat Neurosci. 2011; 14: 452-458. 
  7. Imperatore JA, McAninch DS, Valdez-Sinon AN, et al. FUS recognizes G quadruplex structures within neuronal mRNAs. Frontiers in Molecular Biosciences. 2020; 7: 6. 
  8. Shang J, Ye G, Shi K, et al. Structural basis of receptor recognition by SARS-CoV-2. Nature. 2020; 581: 221-225. 
  9. Garnier C, Devred F, Byrne D, et al. Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid- like aggregates. Sci Rep. 2017; 7: 6812. 
  10. Classen JB. COVID-19, MMR vaccine, and bioweapons. Diabetes & its Complications.2020; 4: 1-8. 
  11. Classen JB. Evidence supporting the hypothesis that the 2019 epidemic of E-vaping acute lung injury (EVALI) was caused in part by COVID-19. Diabetes & Complications. 2020; 4: 1-2. 
  12. Pfizer-Biotech: COVID-19 Vaccine (BNT162, PF-07302048), Vaccines and Related Biological Products Advisory Committee Briefing Document. Meeting Date: 10 December 2020. 
  13. Roundtree IA, Evans ME, Pan, et al. Dynamic RNA modifications in gene expression regulation. Cell. 2017; 169: 1187-1200. 
  14. Classen JB. Review of Vaccine Induced Immune Overload and the Resulting Epidemics of Type 1 Diabetes and Metabolic Syndrome, Emphasis on Explaining the Recent accelerations in the Risk of Prediabetes and other Immune Mediated Diseases. J Mol Genet Med. 2014; S1: 025. 
  15. Amiral J. Can COVID-19 Induce an autoimmune disease associated with long- lasting symptoms and delayed complications? Ann Clin Immunol Microbiol. 2020; 2: 1014. 
  16. Wang EY, Mao T, Klein J, et al. Diverse functional autoantibodies in patients with COVID-19. medRxiv preprint. 2020. 
  17. Lyons-Weiler J. Pathogenic priming likely contributes to serious and critical illness and mortality in COVID-19 via autoimmunity. Journal of Translational Autoimmunity. 2020; 3: 100051. 
  18. Tetz G, Tetz V. SARS-CoV-2 prion-like domains in spike proteins enable higher affinity to ACE2. Preprint. 2020. 
  19. Young MJ, O’Hare M, Matiello M, et al. Creutzfeldt-Jakob disease in a man with COVID-19: SARS-CoV-2-accelerated neuro degeneration? Brain, Behavior, and Immunity. 2020; 89: 601-603. 


Leave a Reply