SARS-CoV-2 impairs the disassembly of stress granules and promotes ALS-associated amyloid aggregation.
Ontology highlight
ABSTRACT: The nucleocapsid (N) protein of SARS-CoV-2 has been reported to have a high ability of liquid-liquid phase separation, which enables its incorporation into stress granules (SGs) of host cells. However, whether SG invasion by N protein occurs in the scenario of SARS-CoV-2 infection is unknow, neither do we know its consequence. Here, we used SARS-CoV-2 to infect mammalian cells and observed the incorporation of N protein into SGs, which resulted in markedly impaired self-disassembly but stimulated cell cellular clearance of SGs. NMR experiments further showed that N protein binds to the SG-related amyloid proteins via non-specific transient interactions, which not only expedites the phase transition of these proteins to aberrant amyloid aggregation in vitro, but also promotes the aggregatio
SUBMITTER: Li Y
PROVIDER: S-EPMC8983322 | biostudies-literature | 2022 Aug
REPOSITORIES: biostudies-literature
ACCESS DATA