Underlying selection for the diversity of spike protein sequences of SARS‐CoV‐2. Issue 3 (25th November 2021)

• Record Type: Journal Article
• Authors: Ghosh, Manisha; Basak, Surajit; Dutta, Shanta
• Is Part Of: IUBMB life. Volume 74:Issue 3(2022)
• Page Start: 213
• Page End: 220
• Publication Date: 2021-11-25
• Subjects: amino acid usage -- correspondence analysis -- hydrophobicity -- molecular docking -- spike protein sequence; Biochemistry -- Periodicals; Molecular biology -- Periodicals; 572.8
• DOI: 10.1002/iub.2577
• Languages: English
• ISSNs: 1521-6543

Abstract

Abstract: The global spread of SARS‐CoV‐2 is fast moving and has caused a worldwide public health crisis. In the present article, we analyzed spike protein sequences of SARS‐CoV‐2 genomes to assess the impact of mutational diversity. We observed from amino acid usage patterns that spike proteins are associated with a diversity of mutational changes and most important underlying cause of variation of amino acid usage is the changes in hydrophobicity of spike proteins. The changing patterns of hydrophobicity of spike proteins over time and its influence on the receptor binding affinity provides crucial information on the SARS‐CoV‐2 interaction with human receptor. Our results also show that spike proteins have evolved to prefer more hydrophobic residues over time. The present study provides a comprehensive analysis of molecular sequence data to consider that mutational variants might play a crucial role in modulating the virulence and spread of the virus and has immediate implications for therapeutic strategies.