>>15075513

Found a prion- HIV connect. Surely NIH/Fauci/gates did too…

Theprion protein has RNA binding and chaperoning properties characteristic of nucleocapsid protein NCP7 of HIV-1

https://pubmed.ncbi.nlm.nih.gov/11278562/

Abstract

Transmissible spongiform encephalopathies are fatal neurodegenerative diseases associated with the accumulation of a protease-resistant form of the prion protein (PrP). Although PrP is conserved in vertebrates, its function remains to be identified. In vitro PrP binds large nucleic acids causing the formation of nucleoprotein complexes resembling human immunodeficiency virus type 1 (HIV-1) nucleocapsid-RNA complexes and in vivo MuLV replication accelerates the scrapie infectious process, suggesting possible interactions between retroviruses and PrP. Retroviruses, including HIV-1 encode a major nucleic acid binding protein (NC protein) found within the virus where 2000 NC protein molecules coat the dimeric genome. NC is required in virus assembly and infection to chaperone RNA dimerization and packaging and in proviral DNA synthesis by reverse transcriptase (RT). In HIV-1, 5'-leader RNA/NC interactions appear to control these viral processes. This prompted us to compare and contrast the interactions of human and ovine PrP and HIV-1 NCp7 with HIV-1 5'-leader RNA. Results show that PrP has properties characteristic of NCp7 with respect to viral RNA dimerization and proviral DNA synthesis by RT. The NC-like properties of huPrP map to the N-terminal region of huPrP. Interestingly, PrP localizes in the membrane and cytoplasm of PrP-expressing cells. These findings suggest that PrP is a multifunctional protein possibly participating in nucleic acid metabolism.

J Biol Chem

. 2001 Jun 1;276(22):19301-9. doi: 10.1074/jbc.M009754200. Epub 2001 Feb 27.

>>15075618

>>15075618

Global Virology I - Identifying and Investigating Viral Diseases pp 575-586

Prion Diseases, HIV-1 Associated Neurocognitive Disorders, and Alzheimer’s Disease: Implications for Protein Misfolding

Abstract

Protein misfolding is a common feature of several neurodegenerative diseases including prion disease, Alzheimer’s disease (AD), and certain forms of HIV associated neurocognitive disorders (HAND). In classical prion disease the cellular prion protein, PrPC, after partial misfolding, converts into a protease-resistant disease-associated isoform, PrPSc, which aggregates in the brain and forms deposits that are associated with the neurodegeneration. Although the phenomenon of PrPC to PrPSc conversion does not occur in HIV infection, protein misfolding in the course of HIV infection has been noted in several preclinical and clinical reports in the form of self-assembling misfolded tau and amyloid-beta (Aβ) proteins. In addition, the misfolding of these proteins are hallmark pathologies of AD. Biomarkers as indicators for the progression of AD and HAND are in need. In this chapter we examine PrPc, Aβ, and, tau and their association with prion biology, protein misfolding, and the possible use of all three proteins for diagnostic and/or prognostic clinical use.

https://link.springer.com/chapter/10.1007/978-1-4939-2410-3_22

>>15075618

>>15075673

>>15075817

>>15075629

https://dpbh.nv.gov/uploadedFiles/dpbhnvgov/content/Boards/BOH/Meetings/2021/SENEFF~1.PDF

Worse Than the Disease? Reviewing Some ==Possible Unintended Consequences of the mRNA Vaccines

Against COVID-19==

Stephanie Seneff1 and Greg Nigh2

1

Computer Science and Artificial Intelligence Laboratory, MIT

ABSTRACT

Operation Warp Speed brought to market in the United States two mRNA vaccines, produced by Pfizer and

Moderna. Interim data suggested high efficacy for both of these vaccines, which helped legitimize Emergency

Use Authorization (EUA) by the FDA. However, the exceptionally rapid movement of these vaccines through

controlled trials and into mass deployment raises multiple safety concerns. In this review we first describe the

technology underlying these vaccines in detail. We then review both components of and the intended biological

response to these vaccines, including production of the spike protein itself, and their potential relationship to a

wide range of both acute and long-term induced pathologies, such as blood disorders, neurodegenerative

diseases and autoimmune diseases. Among thesepotential induced pathologies, we discuss the relevance of

prion-protein-related amino acid sequences within the spike protein. We also present a brief review of studies

supporting the potential for spike protein “shedding”, transmission of the protein from a vaccinated to an

unvaccinated person, resulting in symptoms induced in the latter. We finish by addressing a common point of

debate, namely, whether or not these vaccines could modify the DNA of those receiving the vaccination. While

there are no studies demonstrating definitively that this is happening, we provide a plausible scenario,

supported by previously established pathways for transformation and transport of genetic material, whereby

injected mRNA could ultimately be incorporated into germ cell DNA for transgenerational transmission. We

conclude with our recommendations regarding surveillance that will help to clarify the long-term effects of

these experimental drugs and allow us to better assess the true risk/benefit ratio of these novel technologies.

2006-04-20

Tyrrell Lectureship in Infection and Immunity

Speaker:Dr. Byron Caughey, Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories

Title:Life and death with prions: Mad cows, wasting elk, and cannibals

Host: Dr. Deborah Burshtyn, Medical Microbiology & Immunology

Sponsor: Faculty of Medicine & Dentistry,Alberta Prion Research Instituteand AHFMR

>>15076024

>Dr. Byron Caughey

>cannibals

Caughey at NIH w/ Fauci?

https://www.niaid.nih.gov/research/byron-caughey-phd

Byron Caughey, Ph.D.

https://www.ualberta.ca/immunology-network/seminars/archive.html

Weird how Alberta CAN has so many prion research institutes?

Wendigo land…

>>15076052

>>15076052

>at NIH w/ Fauci?

No way Fauci is unaware of this guy/prion work at NIH

"Chief, TSE/Prion Biochemistry Section"

>>15076000

>where the autists that do the work

not all…

o7

>>15076095