Researchers at the Indian Institute of Technology, Mandi (IIT Mandi) in Himachal Pradesh have revealed the structural features of an important protein in the COVID-19 virus, which will help understand its mechanism of action, its role in spread and disease severity and development of antiviral therapeutics. The findings are published in Current Research in Virological Science.
According to the tem, current COVID-19 treatments simply manage symptoms as the body fights infection in the immune defense system. There are, at present, no confirmed antiviral drugs that can prevent the virus from replicating.
“One route to neutralize any virus is to attack its proteins. Such an approach is true for the COVID-19 virus as well, and scientists around the world are involved in studies to learn- the structure and functions of proteins to understand viral disease and develop drugs that are effective against the virus, ”said Rajanish Giri, Assistant Professor of Biotechnology, IIT Mandi.
This virus contains 16 non -protein proteins (NSP1 – NSP16), of which NSP1 plays an important role in the pathogenicity (ability to cause disease) of the virus.
“NSP1 breaks down host cell proteins and inhibits immune functions. Its importance is understood by the fact that it is also called the ‘host shutoff factor’. Early in 2020, we showed through bioinformatics studies that NSP1 C -terminal region has a tendency to intrinsic disorder between 0.4 to 0.5 scales – just near the threshold of intrinsic disorder prediction.
However, without the experimental studies we are not sure that this 13–180 amino acid region is actually an intrinsically disordered protein region. In general, these regions are opened up by the solution but are multiplied by specific adaptations when binding to specific molecules or partners within host cells, ”said Giri, explaining the new or advances in his previous research.
The IIT Mandi experimental team studied the structural adaptations of SARS-CoV-2 NSP1 under different conditions-in an organic solvent, membrane surrounding and inside liposomes.
Using analytical techniques such as circular dichroism spectroscopy, fluorescence spectroscopy, and molecular dynamics simulations, the researchers demonstrated the dynamic change in IDR adaptation of NSP1, in response to its environments, due to hydrophobic and electrostatic. interactions between protein and the environment.
“Our findings provide important insights into the sequence of the disease NSP1 C-terminal region (residues 131–180) of the SARS-COV2 virus under different environments, which is helpful in understanding on the greater part of NSP1 and partnerships that bind. that is now unknown, ”Giri said.Other team members along with IIT Mandi research scholars Amit Kumar, Ankur Kumar and Prateek Kumar, with Neha Garg from Banaras Hindu University.