Fig. 4: SPR scanning to differentiate selected single residues’ impact onto the SARS-CoV-2 RBD/hACE2 interaction. | Communications Biology

Fig. 4: SPR scanning to differentiate selected single residues’ impact onto the SARS-CoV-2 RBD/hACE2 interaction.

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. 4

A Cartoon shows naturally occurring key RBD mutations in SARS-CoV-2 Omicron (B.1.1.529 and BA.5.2), and distinct residues of SARS-CoV-1 and RaTG13 from those of WT SARS-CoV-2 spike RBD, with their respective locations projected onto the WT SARS-CoV-2 RBD structure (PDB# 6M0J). B SPR measurements of binding affinity of single SARS-CoV-2 RBD mutants of RBM region interacting with hACE2. For each single mutant, the equilibrium dissociation constants (KD) from triplicate measurements were analyzed with BIAcore@ 8 K Evaluation Software (GE Healthcare) by fitting to a 1:1 Langmuir binding model. Purple, red and yellow colors represent mutants distributed in CR1, CR2 and CR3 subdomains respectively as presented in cartoon A. C SPR measurement of binding affinities of single SARS-CoV-2 RBD mutants of non-RBM region for hACE2.

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