Researchers from the Indian Institute of Technology Mandi (IIT-Mandi), Virginia Commonwealth University and the University of South Florida, US, have recently used computational tools to understand an important part of the viral proteome called Intrinsically Disordered Protein Regions (IDPRs).
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Various research groups are racing against time to decode the COVID-19 virus for a cure. The research team is headed by Rajanish Giri, Assistant Professor, School of Basic Sciences, IIT Mandi. The results have recently been published in the journal 'Cellular and Molecular Life Sciences'. The COVID-19 virus essentially consists of the genetic molecule, RNA, enclosed in an envelope made of lipid and proteins. Once in the host, the virus surpasses the host's defence mechanisms and inserts its RNA into the host cells. Then the virus hijacks the host cell machinery to use the viral RNA for production of viral proteins in a process called 'translation', and the infected cell starts generating toxic viral proteins, which leads to various conditions and symptoms.
It is known that proteins provide both structural and functional characteristics to living things and extraneous (viral) proteins can take over the functions of human cells. "In COVID-19, the RNA is translated first into proteins which perform a wide range of functions. Since protein functions depend both on ordered and disordered regions, it is important to understand the whole proteome considering both ordered and disordered proteins", explains Giri. The set of proteins or proteome comprises both ordered regions and disordered regions in proteins.
Giri said, "Intrinsically Disordered Proteins (IDPs), and Intrinsically Disordered Protein Regions (IDPRs) are gaining attention in recent times because they have been discovered to play vital roles in various biological processes." The IDPs and IDPRs have been strongly correlated with the virulence of viruses, and understanding their structure and functions in COVID-19 can help in finding ways to mitigate the effects of the infection. Both the protein structure and non-structure are fundamental things and their knowledge is paramount to understand the virus pathogenesis.
Using computational tools it is possible to investigate the propensities of the proteins and regions that may or may not form the structure. "We have investigated the disordered side of SARS-CoV-2 proteome using a complementary set of computational approaches to check the prevalence of IDPRs in its proteins and to shed some light on their disorder-related functions and also their disorder-based binding motifs, known as molecular recognition features", says Giri.
Speaking of the implication of their finding, Giri added, "Since many IDPs/IDPRs undergo structural changes upon association with their physiological partners, our study generates important grounds for better understanding of the functionality of these proteins, their interactions with other viral proteins, as well as interaction with host proteins in different physiological conditions."
