LATEST! COVID-19 Research: Study Shows That N-Protein Of SARS-CoV-2 Forms Biomolecular Condensates To Spread Virions And Viral Proteins To Nearby Cells
: A new study by researchers from the Department of Biochemistry and Molecular Biology at Colorado State University have made a breakthrough in discovering that the N proteins of the SARS-C0V-2 coronavirus is able to form biomolecular condensates that helps the spread of virions and viral proteins to nearby healthy host cells.
The study by Dr Eric Ross and Dr Sean Cascarina, biochemistry and molecular biology researchers at Colorado State University, are published in The Federation Of American Societies for Experimental Biology (FASEB) Journal. https://faseb.onlinelibrary.wiley.com/doi/full/10.1096/fj.202001351
The researchers identified a protein encoded by SARS-CoV-2, the virus that causes COVID-19, is believed to be associated with the quick spread of the virus through cells in the human body.
By utilizing the powerful application of the foundational sciences and bioinformatic analysis, their research highlights key characteristics of the virus that could one day be important in the development of a treatment for COVID-19.
Prior to the COVID19 pandemic, both Dr Ross and Dr Cascarina had been studying prions which are misfolded proteins that can transmit their abnormal shape onto normal variants of the same protein.
It is known that prions cause several fatal and transmissible neurodegenerative diseases, including Mad Cow Disease in cattle and Creutzfeldt-Jakob disease in humans.
Dr Cascarina's sub-focus has been on low-complexity domains ie regions in a protein's sequence that differ from typical regions in their amino acid composition and chemical behavior.
Significantly, these low-complexity protein domains have a tendency toward liquid-liquid phase separation, similar to oil separating from water. Some of these proteins form "biomolecular condensates" in a cell, which are small areas in a cell where the protein is highly-concentrated, analogous to the oil droplets that form when oil separates from water.
In their studies Dr Ross and Dr Cascarina of COVID-19 earlier this year, they found that the nucleocapsid, or N, protein in the SARS-CoV-2 virus has a low-complexity domain that may utilize liquid-liquid phase separation to facilitate the packaging of viral RNA into new virus particles that can infect neighboring cells.
This N protein may also be associated with reducing an infected cell's anti-viral stress response. Cells often form something called stress granules, a type of biomolecular condensate, to respond to a change in their environment, and these granules may have an anti-viral effect.
Dr Ross told Thailand Medical News, "The cell can react to a stress event by making changes in the cellular environment including making these modifications to some proteins."
Dr Cascarina added, "But viruses obviously want to avoid a cell's defenses. They want to be infectious, so sometimes they are able to regulate these stress granules."
It has been observed by hijacking the normal stress response; the virus may be able to reduce the cell's anti-viral respons
Ever since the publications of their research paper on, four other labs across America have confirmed parts of Cascarina's hypothesis about the N protein.
In one article that Thailand Medical News had published yesterday as to how the SARS-CoV-2 coronavirus forms filopodia structures to infect nearby cells with virions or viral proteins, the formation of these condensates by the N proteins was found to be true. https://www.thailandmedical.news/news/breaking-covid-19-research-scientist-discover-unusual-way-sars-cov-2-infects-other-cells-once-inside-human-host-without-need-of-receptors
The unique application of these study findings could be for the development of treatments once a person has already contracted the virus, rather than preventing infection like a vaccine. Both of these areas of research are essential to slowing and ending the COVID-19 pandemic.
Proposed models for the influence of the SARS‐CoV‐2 N protein on the formation and regulation of biomolecular condensates. A, Putative or directly observed interactions between the SARS‐CoV‐2 N protein and stress granule (SG) components. B, Three possible models for how the N protein of SARS‐CoV‐2 could affect stress granules in host cells: (1) N protein could be recruited to canonical host cell stress granules, which could have subtle or no effect on stress granules (“passive observer”), or could alter stress granule function by contributing to translation suppression, altering stress granule interactions, or remodeling stress granules; (2) N protein could recruit specific stress granule components to form unique, SARS‐specific stress granules that could serve as sites of viral translation or replication; or (3) N protein could inhibit the formation of canonical host cell stress granules by sequestering critical stress granule components. SARS‐CoV‐2 may inhibit the typical stress granule‐associated antiviral responses in host cells by suppressing downstream events that activate IFN‐β expression. Additionally, the features of the SARS‐CoV‐2 N protein that facilitate interaction with stress granules may also facilitate biomolecular condensation of N protein and genomic RNA during nascent virion formation at the ER‐Golgi intermediate compartment (ERGIC)
Dr Ross added, "From a medical perspective, if you could counteract the virus' ability to interfere with a cell's immune response, then you could help the cells to fight off the virus. I think this falls into the category of very basic science ie if we understand the viral process, then conceivably we can try to design a drug that reverses that process."
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