Journal Article

FZJ-2024-00734

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Tau protein aggregation associated with SARS-CoV-2 main protease

Eberle, R. J. (Corresponding author)FZJ* ; Coronado, M. A.FZJ* ; Gering, I.FZJ* ; Sommerhage, S.FZJ* ; Korostov, K.FZJ* ; Stefanski, A. ; Stühler, K. ; Kraemer-Schulien, V.FZJ* ; Blömeke, L.FZJ* ; Bannach, O.FZJ* ; Willbold, D.FZJ*

2023
PLOS San Francisco, California, US

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Please use a persistent id in citations: doi:10.1371/journal.pone.0288138  doi:10.34734/FZJ-2024-00734

Abstract: The primary function of virus proteases is the proteolytic processing of the viral polyprotein. These enzymes can also cleave host cell proteins, which is important for viral pathogenicity, modulation of cellular processes, viral replication, the defeat of antiviral responses and modulation of the immune response. It is known that COVID-19 can influence multiple tissues or organs and that infection can damage the functionality of the brain in multiple ways. After COVID-19 infections, amyloid-β, neurogranin, tau and phosphorylated tau were detected extracellularly, implicating possible neurodegenerative processes. The present study describes the possible induction of tau aggregation by the SARS-CoV-2 3CL protease (3CLpro) possibly relevant in neuropathology. Further investigations demonstrated that tau was proteolytically cleaved by the viral protease 3CL and, consequently, generated aggregates. However, more evidence is needed to confirm that COVID-19 is able to trigger neurodegenerative diseases.

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Contributing Institute(s):

1. Strukturbiochemie (IBI-7)

Research Program(s):

1. 5244 - Information Processing in Neuronal Networks (POF4-524) (POF4-524)

Appears in the scientific report 2023

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