IIT Mandi Study Explains C-Terminal Part of Covid Virus Key Protein NSP1 in Host Cell, Health News, ET HealthWorld
The results of the research were published in the journal “ Current Research in Virological Science ” in an article authored by lead researcher Dr Rajanish Giri, assistant professor at the School of Basic Sciences and his co-authors Amit Kumar, Ankur Kumar and Prateek Kumar, with Dr Neha Garg from the Hindu University of Banaras.
âCurrent treatments for Covid-19 simply manage symptoms while the body fights infection with its immune defense system. There are not yet any confirmed antiviral drugs that can prevent the virus from replicating. One way to neutralize a virus is to attack its virus. proteins; such an approach is true for the Covid-19 virus, âthe statement said.
Elucidating the structure and functions of these proteins is important for understanding viral disease and for the development of effective drugs against the virus.
Dr Rajanish Giri, Assistant Professor of Biotechnology, IIT Mandi explained, âFrom a conformational or ‘shape’ point of view, many proteins contain ordered and inherently disordered regions. These classic conformations are also found in the proteins of the SARS-CoV-2 virus. The structure of nonstructural protein 1 (NSP1) is made up of 180 amino acids. The first region 1-127 has been shown experimentally to form an independent structure by Clrak, Green & Petit of the University of Alabama. However, there was no experimental evidence given by any group on the 131-180 amino acid regions of this NSP1 protein, which plays a key role in suppressing the host’s immune system. With the support of circular dichroism spectroscopy and molecular dynamics simulations, our group at IIT Mandi deciphered the conformation of this region in isolation.
âThis virus has sixteen non-structural proteins (NSP1 – NSP16), of which NSP1 plays a vital role in the pathogenicity (ability to cause disease) of the virus. NSP1 disrupts the proteins of the host cell and suppresses its immune system Its importance can be understood from the fact that it is also called the “ host stopping factor ”. In particular, Nenad Ban and colleagues found that if the C-terminal region of NSP1, i.e. 131-180 residues, is removed from NSP1, then NSP1 is unable to stop translation by ribosomes. It is therefore important to understand the molecular mechanisms, biophysical interactions and chemistry of the interaction of NSP1 with the host cell, âthe statement added.
âEarlier in 2020, we showed through bioinformatics studies that the C-terminal NSP1 region has a propensity for intrinsic disorders between 0.4 and 0.5 scales, i.e. very close to the limit of the prediction of intrinsic disorders. However, without experimental studies, we were not sure that this 131-180 amino acid region is in fact an inherently disordered protein region. Generally, these regions unfold in solution but fold into particular conformations upon binding with specific molecules or partners inside host cells â, Dr Rajanish Giri added while explaining recent developments in his past research.
“The IIT Mandi team experimentally studied the structural conformations of SARS-CoV-2 NSP1 under various conditions – in an organic solvent, a membrane mimetic environment and inside liposomes. Using analytical techniques such as spectroscopy at Circular dichroism, fluorescence spectroscopy and molecular dynamics simulations, the researchers showed the dynamic changes in the conformation of the IDR of NSP1, in response to its environment, due to hydrophobic and electrostatic interactions between the protein and the environment Â», Specifies the press release.
“Our discovery provides valuable information on the order-of-disorder conformation of the C-terminal NSP1 region (residues 131-180) of the SARS-COV2 virus in various environments, which will help to understand the broader aspect of NSP1 and its interactions with binding partners. which are currently unknown, âsaid Dr Giri.