Identification and molecular characterization of mutations in nucleocapsid phosphoprotein of SARS-CoV-2
Open Access
- 4 January 2021
- Vol. 9, e10666
- https://doi.org/10.7717/peerj.10666
Abstract
SARS-CoV-2 genome encodes four structural proteins that include the spike glycoprotein, membrane protein, envelope protein and nucleocapsid phosphoprotein (N-protein). The N-protein interacts with viral genomic RNA and helps in packaging. As SARS-CoV-2 spread to almost all countries worldwide within 2–3 months, it also acquired mutations in its RNA genome. Therefore, this study was conducted with an aim to identify the variations present in N-protein of SARS-CoV-2. Here, we analysed 4,163 reported sequence of N-protein from United States of America (USA) and compared them with the first reported sequence from Wuhan, China. Our study identified 107 mutations that reside all over the N-protein. Further, we show the high rate of mutations in intrinsically disordered regions (IDRs) of N-protein. Our study show 45% residues of IDR2 harbour mutations. The RNA-binding domain (RBD) and dimerization domain of N-protein also have mutations at key residues. We further measured the effect of these mutations on N-protein stability and dynamicity and our data reveals that multiple mutations can cause considerable alterations. Altogether, our data strongly suggests that N-protein is one of the mutational hotspot proteins of SARS-CoV-2 that is changing rapidly and these mutations can potentially interferes with various aspects of N-protein functions including its interaction with RNA, oligomerization and signalling events.Funding Information
- The author received no funding for this work. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript
This publication has 43 references indexed in Scilit:
- Oligomerization of the carboxyl terminal domain of the human coronavirus 229E nucleocapsid proteinFEBS Letters, 2012
- Inhibition of influenza virus replication via small molecules that induce the formation of higher-order nucleoprotein oligomersProceedings of the National Academy of Sciences of the United States of America, 2011
- Coronavirus Nucleocapsid Protein Facilitates Template Switching and Is Required for Efficient TranscriptionJournal of Virology, 2010
- Coronavirus nucleocapsid protein is an RNA chaperoneVirology, 2006
- Immunological characterizations of the nucleocapsid protein based SARS vaccine candidatesVaccine, 2006
- Characterization and application of monoclonal antibodies against N protein of SARS-coronavirusBiochemical and Biophysical Research Communications, 2005
- UCSF Chimera?A visualization system for exploratory research and analysisJournal of Computational Chemistry, 2004
- WebLogo: A Sequence Logo Generator: Figure 1Genome Research, 2004
- Identification of an epitope of SARS-coronavirus nucleocapsid proteinCell Research, 2003
- Phosphorylation of the Porcine Reproductive and Respiratory Syndrome Virus Nucleocapsid ProteinJournal of Virology, 2002