Higher infectivity of the SARS‐CoV‐2 new variants is associated with K417N/T, E484K, and N501Y mutants: An insight from structural data

• Published in: Journal of cellular physiology Vol. 236; no. 10; pp. 7045 - 7057
• Main Authors: Khan, Abbas, Zia, Tauqir, Suleman, Muhammad, Khan, Taimoor, Ali, Syed Shujait, Abbasi, Aamir Ali, Mohammad, Anwar, Wei, Dong‐Qing
• Format: Journal Article
• Language: English
• Published: United States Wiley Subscription Services, Inc 01.10.2021; John Wiley and Sons Inc
• Subjects: ACE2; Angiotensin-converting enzyme 2; Angiotensin-Converting Enzyme 2 - metabolism; Binding; Brazil; COVID-19; COVID-19 - metabolism; Dynamic structural analysis; Epistasis; Evolution; Free energy; Glycoproteins; Humans; In vivo methods and tests; Infectivity; KD (dissociation constant); MD simulation; Mutants; Mutation; Mutation - genetics; new variants; Pathogenicity; Pathogens; Protein Binding - genetics; Proteins; protein–protein docking; Receptors; SARS-CoV-2 - genetics; SARS‐CoV‐2; Severe acute respiratory syndrome; Severe acute respiratory syndrome coronavirus 2; South Africa; Spike glycoprotein; Spike protein; United Kingdom; Virulence; Virulence - genetics; Brazil; South Africa; United Kingdom; United Kingdom > UK; MD simulation; new variants; SARS-CoV-2; protein-protein docking; KD (dissociation constant)

The evolution of the SARS‐CoV‐2 new variants reported to be 70% more contagious than the earlier one is now spreading fast worldwide. There is an instant need to discover how the new variants interact with the host receptor (ACE2). Among the reported mutations in the Spike glycoprotein of the new va...