datum (n=1)This paper: https://pubs.acs.org/doi/10.1021/acschemneuro.5c00478
Our results indicate that [COVID Spike proteins] can [...] cause lipid vesicle leakage and exhibit increased toxicity to neuroblastoma cells
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our findings raise compelling questions about the potential role of SARS-CoV-2 infection in accelerating or triggering neurodegenerative diseases linked to protein amyloidosis
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Emerging evidence suggests that the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection may have long-term deleterious effects on the central nervous system and even contribute to post-COVID neurological syndromes
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Several theoretical and experimental studies have suggested that certain proteins from the SARS-CoV-2 virus can promote, either directly or indirectly, the formation of amyloid aggregates. For instance, the S1 domain of SARS-CoV-2, which includes the fragment S194, has been shown to interact with αSyn, inducing the formation of protein aggregates capable of causing synaptic damage and cytotoxicity
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H1N1 infection has been reported to [...] increasing susceptibility to neurodegeneration
#COVID #COVID19 #SARSCoV2 #neurodegeneration #neurology #nueroscience #CovidIsNotOver
An Amyloidogenic Fragment of the Spike Protein from SARS-CoV-2 Virus Stimulates the Aggregation and Toxicity of Parkinson’s Disease Protein Alpha-Synuclein
Emerging evidence suggests that the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection may have long-term deleterious effects on the central nervous system and even contribute to post-COVID neurological syndromes. Interestingly, inflammation-induced proteolytic processing of the Spike protein of SARS-CoV-2 leads to the generation of peptides capable of aggregating into amyloid fibrils in vitro. Herein, we investigate the in vitro effect of a fibrillogenic fragment of the Spike protein [Spike 194–203 (S194)] on the aggregation and toxicity of the Parkinson’s disease (PD) protein α-synuclein (αSyn). Our results indicate that S194 fibrils stimulate in a concentration-dependent manner the fibrillation of αSyn monomer, resulting in aggregates with increased capacity of inducing lipid vesicle leakage and toxicity to neuroblastoma cells, in comparison with either αSyn or S194 alone. Bidimensional NMR (1H–15N-HSQC) suggests that S194 fibrils cause a higher perturbation in both the N-terminal region (sequence: 19–68) and the hydrophobic central domain of the αSyn monomer (sequence: 71–95), which is corroborated by protein–peptide docking and molecular dynamics simulations. In contrast with fibrils from wild-type αSyn, aggregates from the PD variant A30P exhibited a remarkable accelerative effect on S194 fibrillation. Similarly, fibrils from amyloid-β peptides, which are linked to Alzheimer’s disease, exhibited a pro-aggregating effect on the S194 monomer. Taken together, these findings might contribute to a broader understanding of the potential connections between SARS-CoV-2 infection and amyloid-related neurodegenerative disorders, highlighting areas that may warrant further investigation.
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