Abstract
The SARS-CoV-2 variant Omicron is characterized, among others, by more than 30 amino acid changes occurring on the spike glycoprotein with respect to the original SARS-CoV-2 spike protein. We report a comprehensive analysis of the effects of the Omicron spike amino acid changes in the interaction with human antibodies, obtained by modeling them into selected publicly available resolved 3D structures of spike-antibody complexes and investigating the effects of these mutations at structural level. We predict that the interactions of Omicron spike with human antibodies can be either negatively or positively affected by amino acid changes, with a predicted total loss of interactions only in a few complexes. Moreover, our analysis applied also to the spike-ACE2 interaction predicts that these amino acid changes may increase Omicron transmissibility. Our approach can be used to better understand SARS-CoV-2 transmissibility, detectability, and epidemiology and represents a model to be adopted also in the case of other variants.
Keywords: SARS-CoV-2; antibodies; protein variants; protein–protein interactions; spike.
【저자키워드】 antibodies, SARS-CoV-2, spike, protein variants, protein–protein interactions, 【초록키워드】 Mutation, antibody, Epidemiology, spike glycoprotein, SARS-CoV-2 variant, omicron, Spike protein, Protein, Transmissibility, SARS-CoV-2 spike protein, detectability, 3D structure, predict, Amino acid, Interaction, Analysis, amino acid changes, protein–protein interactions, among others, comprehensive analysis, other variants, Effect, approach, selected, predicted, amino acid change, affected, applied, characterized, can be used, adopted, complexes, resolved, 【제목키워드】 spike, Human, change, acid, Effect,