Journal
PROTEIN JOURNAL
Volume 40, Issue 3, Pages 328-340Publisher
SPRINGER
DOI: 10.1007/s10930-021-09988-3
Keywords
SARS-CoV-2 proteins; Mutation stability; Clustering; Shannon entropy; Mutation profiling
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Funding
- FRPDF grant of Presidency University
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This study utilized in silico experiments to investigate the mutational profiling and evolutionary aspects of various coronavirus proteins, shedding light on the impact of mutations on protein stability and function, as well as their significance in the evolution of SARS-CoV-2.
Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), an enveloped RNA virus transmits by droplet infection thus affects the respiratory system. Different genomes have been reported globally for SARS-CoV-2 with moderate level of mutation which makes it harder to combat the virus. Mutational profiling and the relevant evolutionary aspect of coronavirus proteins namely spike glycoprotein, membrane protein, envelope protein, nucleoprotein, ORF1ab, ORF3a, ORF6, ORF7a, ORF7b and ORF8 were studied by in silico experiments. Clustering of the protein sequences and calculation of residue relative abundance were done to get an idea about the protein conservancy as well as finding out some representative sequences for phylogenetic and ancestral reconstruction. By mutational profiling and mutation analysis, the effect of mutations on the protein stability and their functional implication were studied. This study indicates the mutational effect on the proteins and their relevance in evolution, which directs us towards a better understanding of these variations and diversification of SARS-CoV-2 for useful future therapeutic study and thus aid in designing therapeutic agents keeping the highly variable regions in mind.
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