Researchers from Munich and Ulm have been trying to understand the virus better and have determined how coronavirus SARS-CoV-2 inhibits the synthesis of proteins in infected cells and effectively disarms the body’s innate immune system. This Nonstructural Protein 1 (Nsp1) encoded by the coronavirus SARS-Cov-2 has been revealed to have a damaging effect on host cells. It is one of the central weapons used to reproduce in human hosts. Nsp1 has been identified as a virulence factor after a related SARS coronavirus outbreak nearly 20 years ago when it was shown to inhibit protein synthesis in infected cells.
Researchers based at Ludwig-Maximilians-Universitaet (LMU) and Ulm University Hospital have revealed what makes Nsp1 so vigorous. The task of synthesizing proteins in all cells is performed by complex molecular machines known as ribosomes. Ribosomes interact with RNAs (mRNAs), which serve as plans for protein synthesis and translate the nucleotide sequence of each mRNA into the amino-acid sequence of the corresponding protein. Ribosomes consist of two different subunits, and Nsp1 binds to the smaller one – the 40S subunit. The mRNA initially binds to the small subunit, before the interaction with the 60S subunit to form the cavity.
The new research reveals that one end of the Nsp1 protein interacts with the 40S subunit in such a way that it prevents the binding of the mRNA. Researchers hope that this will make it possible to find ways to neutralize the novel coronavirus and mitigate the severity of the respiratory disease that it causes.
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