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Persistent Spike

Unraveling the enigma of long COVID: novel aspects in pathogenesis, diagnosis, and treatment protocols

“Unraveling the enigma of long COVID: novel aspects in pathogenesis, diagnosis, and treatment protocols” published in Inflammopharmacology is a comprehensive review exploring the complex nature of long COVID. https://link.springer.com/article/10.1007/s10787-024-01483-2  

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Pseudouridine, mRNA Vaccines & Spike Protein Persistence

The mRNA vaccines developed by Pfizer and Moderna for COVID-19 contain engineered mRNA encoding the spike protein of the SARS-CoV-2 virus. This mRNA differs slightly from the viral mRNA, employing a stabilizing modification using pseudouridine. Recent studies have shown that the vaccine mRNA can persist in the body for several weeks, raising questions about potential

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SARS-CoV-2, long COVID, prion disease and neurodegeneration

The evidence suggests a strong link between SARS-CoV-2 infection, long COVID, and the development or acceleration of neurodegenerative diseases. The mechanisms underlying this relationship appear to involve the prion-like properties of the SARS-CoV-2 spike protein, shared inflammatory pathways, and the widespread distribution of the ACE2 receptor in the brain. Further research is needed to fully

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SARS-COV-2 Spike Protein causes prionlike diseases

Based on the additional search results provided, the key information about the “spike532” sequence and its relation to prion protein biogenesis is: The spike532 sequence refers to a specific region within the SARS-CoV-2 spike protein that has been identified as having prion-like properties[2]. Specifically, the search results indicate that the spike532 sequence contains signal sequences

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PrP aggregation can be seeded by pre-formed recombinant PrP amyloid fibrils without the replication of infectious prions

We show that inoculation of recPrP fibrils does not cause TSE disease, but, instead, seeds the formation of PrP amyloid plaques in PrP-P101L knock-in transgenic mice (101LL). Importantly, both WT-recPrP fibrils and 101L-recPrP fibrils can seed plaque formation, indicating that the fibrillar conformation, and not the primary sequence of PrP in the inoculum, is important

PrP aggregation can be seeded by pre-formed recombinant PrP amyloid fibrils without the replication of infectious prions Read More »

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