Abstract
The prefatory protein-glycan interaction and stabilizing protein-protein interaction of severe acute respiratory syndrome viruses with angiotensin-converting enzyme 2 play a significant role in complex formation thereby promoting endocytosis. The microevolution of SARS-CoV-2 over a period of time has a significant role in increasing the affinity of receptor-binding domain against angiotensin converting-enzyme 2. In the current study, we have corroborated the vitality of acquired SNPs over a period of time with increased affinity by using docking studies. The results indicate that the virus modulates the undesirable glycosylation sites by a series of substitution and deletion mutations. It uses bulky residues such as Tyr/Phe for dynamic arrest for quick stabilization of the complex, and Lys residues for stabilizing via hydrogen bond formation besides increasing the binding affinity to ease the cell entry.
Competing Interest Statement
The authors have declared no competing interest.
Abbreviations
- ACE2
- Angiotensin Converting Enzyme 2
- CNI
- Close-Neighbor-Interchange
- CoV
- Corona Virus
- HADDOCK
- High Ambiguity Driven Protein-Protein Docking
- LC-MS
- Liquid Chromatography - Mass Spectroscopy
- Pangolin
- Phylogenetic Assignment Of Named Global Outbreak Lineages
- PGI
- Protein-Glycan Interactions
- RBD
- Receptor Binding Domain
- PPI
- Protein-Protein Interactions
- SARS
- Severe Acute Respiratory Syndrome
- SASA
- Solvent Accessible Surface Area
- SNP
- Single Nucleotide Polymorphism
- VOC
- Variant Of Concern