Fig. 3: Scheme of the natural mutations distributed on RBD, especially on the RBM of SARS-CoV-2 and RBD/hACE2 binding affinities’ comparison among representative world-wide circulating SARS-CoV-2 VOCs. | Communications Biology

Fig. 3: Scheme of the natural mutations distributed on RBD, especially on the RBM of SARS-CoV-2 and RBD/hACE2 binding affinities’ comparison among representative world-wide circulating SARS-CoV-2 VOCs.

From: Interfacial subregions of SARS-CoV-2 spike RBD to hACE2 affect intermolecular affinity by their distinct roles played in association and dissociation kinetics

Fig. 3

A Top view of the respective SARS-CoV-2 VOCs’ RBM with key residues in contact with hACE2 of WT SARS-CoV-2(top left) or corresponding mutated residues from other VOCs colored accordingly. Also array of key mutated residue locations clustered from all selected VOCs are projected onto the same WT SARS-CoV-2 RBD structure (2nd image on top left). Protein structures of wild type, Alpha(B.1.17), Beta(B.1.351), Gamma(P.1), Delta(B.1.617.2), and Omicron (B.1.1.529, BA.5.2) RBDs are referred to PDB# 6M0J, 7MJN, 7V80, 7NXC, 7WBQ, 7TN0, and 7XWA respectively31,47,50,51,66,67. B Scheme of natural mutations distributed along the SARS-CoV-2 VOCs’ primary RBD protein sequence. For WT SARS-CoV-2 RBD, the RBM sequence coverage is labeled by a two-way arrow. For Omicron (BA.5.2), additional natural mutations to those of Omicron (B.1.1.529) are displayed in deep blue and retro-mutated residues of R493Q and S496G in RBM are colored in green. C RBD binding affinities to hACE2 are compared among selected SARS-CoV-2 VOCs by triplicate SPR measurements each. D Measurement of the impact on the SARS-CoV-2 RBD/hACE2 interaction by CR1, CR2 and CR3 swapped from Omicron (BA.5.2) respectively. Alongside is a SPR scan of Omicron (B.1.1.529) RBD chimera with CR3 swapped from SARS-CoV-1 to further corroborate CR3’s dominant role in high affinity RBD/hACE2 interaction.

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