期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 78, 期 4, 页码 1655-1688出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-020-03603-x
关键词
SARS coronavirus; Intrinsically disordered proteins; Molecular recognition features; Nucleotide-binding regions; Coronavirus disease 2019
资金
- MHRD
- Department of Biotechnology (DBT), India [BT/PR16871/NER/95/329/2015]
- IIT Mandi-IIT Ropar-PGI Chandigarh, BioX consortium grant [IITM/INT/RG/18]
- Department of Science and Technology
The emergence of SARS-CoV-2, leading to COVID-19, has become a global public health emergency. Research shows that the SARS-CoV-2 proteome exhibits significant levels of structural order, with functionally important intrinsically disordered protein regions playing a crucial role in viral infectivity and pathogenicity.
The recently emerged coronavirus designated as SARS-CoV-2 (also known as 2019 novel coronavirus (2019-nCoV) or Wuhan coronavirus) is a causative agent of coronavirus disease 2019 (COVID-19), which is rapidly spreading throughout the world now. More than 1.21 million cases of SARS-CoV-2 infection and more than 67,000 COVID-19-associated mortalities have been reported worldwide till the writing of this article, and these numbers are increasing every passing hour. The World Health Organization (WHO) has declared the SARS-CoV-2 spread as a global public health emergency and admitted COVID-19 as a pandemic now. Multiple sequence alignment data correlated with the already published reports on SARS-CoV-2 evolution indicated that this virus is closely related to the bat severe acute respiratory syndrome-like coronavirus (bat SARS-like CoV) and the well-studied human SARS coronavirus (SARS-CoV). The disordered regions in viral proteins are associated with the viral infectivity and pathogenicity. Therefore, in this study, we have exploited a set of complementary computational approaches to examine the dark proteomes of SARS-CoV-2, bat SARS-like, and human SARS CoVs by analysing the prevalence of intrinsic disorder in their proteins. According to our findings, SARS-CoV-2 proteome contains very significant levels of structural order. In fact, except for nucleocapsid, Nsp8, and ORF6, the vast majority of SARS-CoV-2 proteins are mostly ordered proteins containing less intrinsically disordered protein regions (IDPRs). However, IDPRs found in SARS-CoV-2 proteins are functionally important. For example, cleavage sites in its replicase 1ab polyprotein are found to be highly disordered, and almost all SARS-CoV-2 proteins contains molecular recognition features (MoRFs), which are intrinsic disorder-based protein-protein interaction sites that are commonly utilized by proteins for interaction with specific partners. The results of our extensive investigation of the dark side of SARS-CoV-2 proteome will have important implications in understanding the structural and non-structural biology of SARS or SARS-like coronaviruses.
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