Nature Sub-Journal: Revealing new mechanisms for coronavirus to intercept host cells to make viruses is expected to help develop new therapies and vaccines.

September 16, 2020 // -- In a recent study published in the international journal Nature Structural and Molecular Biology, scientists from the Federal Institute of Technology in Zurich and others revealed new molecular mechanisms by which coronavirus manipulates human cells to replicate the virus itself;
photo source: David S. Goodsell, RCSB Protein Data Bank, like pirate hijackers, controls infected cells because each virus relies on resources and molecular machines in the cells to replicate, which also applies to SARS-CoV-2, which causes COVID-19; The new mechanism, which makes coronavirus more likely to produce its own protein than the protein the cell itself needs, also causes cells to significantly reduce the synthesis of their own proteins, and almost only produce viral proteins, which not only promote the production of new viruses, but also inhibit the host body's immune response against coronavirus infection.
During SARS-CoV-2 infection, when the virus enters the host cell, the viral protein NSP1 is produced as the first viral protein, and studies of other coronavirus have found that NSP1 inhibits the production of the cell's own protein, but researchers do not yet know exactly how the process occurs;
Nrucleosomes are cellular machines that help proteins produce information that reads mRNA information and assembles synthetic amino acids in the order in which mRNA passes through a channel on the RNA, which the researchers say NSP1 binds to block the function of the RNA, using cryogenic electroscopy technology that allows researchers to perform at atomic resolution. The binding points of NSP1 on the cytomeome are revealed, and detailed images can also provide researchers with important information to help later develop new drugs that potentially inhibit NSP1 binding without interfering with the function of the nSP1, which activates the host body's cell defense system to block the replication process of the virus if it no longer interacts with the CYG.
Through bio-chemical and cellular experiments, the researchers say that NSP1 alone is enough to inhibit protein production, and based on detailed map information on the NPS1 binding pattern, the researchers were able to create modified, loss-inhibiting NSP1 mutants, and that SARS-CoV-2, which carries NSP1 incapaated mutants, might potentially be snredated so that it could not induce serious diseases, and that such detoxification viruses could be potentially used to develop new vaccines.
In addition, the researchers are interested in studying why, despite NPS1's ability to inhibit the function of the RNA, the virus's proteins are still produced in large quantities, and they have found that the virus's RNA has unique characteristics compared to cell mRNAs so that the RNA can read it effectively, and through N SP1 blocks the function of the RNA, the functional RNA becomes scarce, and the virus's RNA produces nearly half of the RNA in the cell;
() Original source: Schubert, K., Karousis, E.D., Jomaa, A. et al. SARS-CoV-2 Nsp1 binds the ribosomal mRNA channel to resed. Nat Struct Mol Biol (2020). doi:10.1038/s41594-020-0511-8.