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10.1021/acschemneuro.1c00666

http://scihub22266oqcxt.onion/10.1021/acschemneuro.1c00666
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suck abstract from ncbi


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pmid34860005      ACS+Chem+Neurosci 2022 ; 13 (1): 143-150
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  • Interactions between SARS-CoV-2 N-Protein and alpha-Synuclein Accelerate Amyloid Formation #MMPMID34860005
  • Semerdzhiev SA; Fakhree MAA; Segers-Nolten I; Blum C; Claessens MMAE
  • ACS Chem Neurosci 2022[Jan]; 13 (1): 143-150 PMID34860005show ga
  • First cases that point at a correlation between SARS-CoV-2 infections and the development of Parkinson's disease (PD) have been reported. Currently, it is unclear if there is also a direct causal link between these diseases. To obtain first insights into a possible molecular relation between viral infections and the aggregation of alpha-synuclein protein into amyloid fibrils characteristic for PD, we investigated the effect of the presence of SARS-CoV-2 proteins on alpha-synuclein aggregation. We show, in test tube experiments, that SARS-CoV-2 spike protein (S-protein) has no effect on alpha-synuclein aggregation, while SARS-CoV-2 nucleocapsid protein (N-protein) considerably speeds up the aggregation process. We observe the formation of multiprotein complexes and eventually amyloid fibrils. Microinjection of N-protein in SH-SY5Y cells disturbed the alpha-synuclein proteostasis and increased cell death. Our results point toward direct interactions between the N-protein of SARS-CoV-2 and alpha-synuclein as molecular basis for the observed correlation between SARS-CoV-2 infections and Parkinsonism.
  • |*Amyloid/metabolism[MESH]
  • |*alpha-Synuclein/metabolism[MESH]
  • |COVID-19[MESH]
  • |Coronavirus Nucleocapsid Proteins/*metabolism[MESH]
  • |Humans[MESH]
  • |Phosphoproteins/metabolism[MESH]
  • |SARS-CoV-2[MESH]


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