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Advancing High-Resolution Imaging of Virus Assemblies in Liquid and Ice
Published on: July 20, 2022
Coupling of SARS-CoV-2 to Amyloid Fibrils and Liquid-Liquid Phase Separation
Hoang Linh Nguyen1,2, Mai Suan Li3
1Institute of Fundamental and Applied Sciences, Duy Tan University, Ho Chi Minh City, 700000, Vietnam.
Abstract:
COVID-19 is a respiratory disease caused by Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), but because the receptor protein of this virus can appear not only in the lungs and throat but also in various parts of the host's body, it causes different diseases. Recent observations have suggested that SARS-CoV-2 damages the central nervous system of patients in a manner similar to amyloid-associated neurodegenerative diseases such as Alzheimer's and Parkinson's. Neurodegenerative diseases are believed to be associated with the self-assembly of amyloid proteins and peptides. On the other hand, whole proteins or parts of them encoded by SARS-CoV-2 can form amyloid fibrils, which may play an important role in amyloid-related diseases. Motivated by this evidence, this mini-review discusses experimental and computational studies of SARS-CoV-2 proteins that can form amyloid aggregates. Liquid-Liquid Phase Separation (LLPS) is a dynamic and reversible process leading to the creation of membrane-less organelles within the cytoplasm, which is not bound by a membrane that concentrates specific types of biomolecules. These organelles play pivotal roles in cellular signaling, stress response, and the regulation of biomolecular condensates. Recently, LLPS of the Nucleocapsid (N) protein and SARS-CoV-2 RNA has been disclosed, but many questions about the phase separation mechanism and the formation of the virion core are still unclear. We summarize the results of this phenomenon and suggest potentially intriguing issues for future research.
Insights
Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) proteins can form amyloid aggregates, potentially linking COVID-19 to neurodegenerative diseases. This review explores SARS-CoV-2 protein aggregation and liquid-liquid phase separation (LLPS).
Area of Science:
- Molecular biology and virology
- Neuroscience and neurodegenerative diseases
- Biophysics and protein aggregation
Background:
- COVID-19, caused by SARS-CoV-2, affects multiple organs due to viral receptor distribution.
- Emerging evidence links SARS-CoV-2 to neurodegenerative conditions like Alzheimer's and Parkinson's.
- Amyloid protein self-assembly is a hallmark of neurodegenerative diseases.
Purpose of the Study:
- To review experimental and computational studies on SARS-CoV-2 proteins forming amyloid aggregates.
- To discuss the role of liquid-liquid phase separation (LLPS) in SARS-CoV-2.
- To highlight open questions and future research directions in this field.
Main Methods:
- Review of existing experimental studies on SARS-CoV-2 protein aggregation.
- Analysis of computational research investigating amyloid fibril formation by viral proteins.
- Summary of findings related to liquid-liquid phase separation (LLPS) of SARS-CoV-2 components.
Main Results:
- SARS-CoV-2 proteins, including the Nucleocapsid (N) protein, can form amyloid aggregates.
- These viral amyloids may contribute to amyloid-related pathologies and neurodegeneration.
- Liquid-Liquid Phase Separation (LLPS) involving SARS-CoV-2 N protein and RNA has been observed, impacting cellular processes.
Conclusions:
- SARS-CoV-2 proteins have the potential to form amyloid structures, suggesting a link to neurodegenerative diseases.
- Understanding LLPS mechanisms of viral proteins is crucial for elucidating disease pathogenesis and virion formation.
- Further research is needed to clarify the precise role of viral protein aggregation and LLPS in COVID-19 pathogenesis.
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