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Comment
. 2022 Jan 5;7(1):8.
doi: 10.1038/s41392-021-00863-2.

SARS-CoV-2 Omicron RBD shows weaker binding affinity than the currently dominant Delta variant to human ACE2

Leyun Wu #  1 , Liping Zhou #  1 , Mengxia Mo #  2 , Tingting Liu #  3 , Chengkun Wu #  2 , Chunye Gong  2 , Kai Lu  2 , Likun Gong  4 , Weiliang Zhu  5 , Zhijian Xu  6
Affiliations
Comment

SARS-CoV-2 Omicron RBD shows weaker binding affinity than the currently dominant Delta variant to human ACE2

Leyun Wu et al. Signal Transduct Target Ther. .
No abstract available

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Conflict of interest statement

The authors declare no competing interests.

Figures

Fig. 1
Fig. 1
Binding affinity of ACE2 to the RBDs of WT, Delta and Omicron variants. a Mapping SARS-CoV-2 RBD mutations on the three-dimensional structure. The spike protein trimer is shown as surface. Identical mutations sites in both Delta and Omicron variants are shown as magenta. Other RBD mutations in Delta and Omicron variants are shown as green and yellow, respectively. b The predicted ACE2-RBD binding free energy (kcal/mol) of WT, Delta and Omicron variants. c RBD-ACE2 affinity constants measured by ELISA. d The predicted mAb-RBD binding free energy (kcal/mol) of WT, Delta and Omicron variants. e Energy contributions of 16 RBD mutations in Delta or Omicron variants. NS, not significant; *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001
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References

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Supplementary concepts