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April 2024

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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Review: N1-methyl-pseudouridine (m1Ψ): Friend or foe of cancer?

The document titled “Review: N1-methyl-pseudouridine (m1Ψ): Friend or foe of cancer?” authored by Alberto Rubio-Casillas and colleagues, provides a comprehensive review of the role of N1-methyl-pseudouridine (m1Ψ) in the context of cancer, particularly focusing on its implications when used in mRNA vaccines, such as those developed for COVID-19. The review highlights the rapid development and

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Effects of COVID-19 and vaccination on the human immune system: cases of lymphopenia and autoimmunity

The article from Future Virology, authored by J Gerlach and AM Baig, discusses the effects of COVID-19 and vaccination on the human immune system, particularly focusing on cases of lymphopenia and autoimmunity. The study explores the possibility that some individuals may be more prone to developing an immune response to self-antigens after COVID-19 infection and

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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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