Journal of Molecular Biology
Volume 432, Issue 19, 4 September 2020, Pages 5212-5226
Mutations Strengthened SARS-CoV-2 Infectivity
Graphical abstract
More than 8000 observed single mutations in the SARS-CoV-2 genomes have raised serious concerns about changes in infectivity. Qualitatively, such infectivity is proportional to the binding affinity between SARS-CoV-2 spike glycoprotein (S protein) and host ACE2 receptor. This work proposes a machine learning model to evaluate the relative infectivity following the mutations. We show that five out of six SARS-CoV-2 substrains have become more infectious, while the other one becomes less infectious. We found that a few potential future mutations on the S protein could lead to more dangerous new viruses.
Keywords
COVID-19
viral infectivity
spike protein
mutation
protein-protein interaction
Abbreviations
COVID-19
coronavirus disease 2019
SARS-CoV-2
severe acute respiratory syndrome coronavirus 2
ACE2
angiotensin-converting enzyme 2
RBD
receptor-binding domain
PPI
protein–protein interaction
BFE
binding free energy
RBM
receptor-binding motif
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