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. 2023 Nov 22;12:e74060. doi: 10.7554/eLife.74060

Figure 5. Role of residue 417 in direct interaction with ACE2 receptor.

(A) Lys417 in SARS-CoV-2 receptor-binding domain (RBD) forms a favorable salt bridge with Asp30 in human ACE2. PDB code: 6M0J. (B) Val404 in SARS-CoV-1 RBD (whose position is equivalent to residue 417 in SARS-CoV-2 RBD) does not form any direct interaction with human ACE2. PDB code: 2AJF. (C) Flow cytometry assay to detect the interactions between recombinant SARS-CoV-2 RBD and cell-surface-anchored human ACE2 (Figure 5—source data 1). The RBD contains either Lys417 (wild-type residue) or Val417 (mutant residue). MFI: median fluorescence intensity. See Figure 5—figure supplement 1 for details of this experiment. Data are mean + SEM. A comparison (two-tailed Student’s t-test) was performed on data between indicated groups (n = 3). ***p<0.001. This experiment was repeated independently three times with similar results.

Figure 5—source data 1. Numerical data for Figure 5C.

Figure 5.

Figure 5—figure supplement 1. Flow cytometry assay on the interactions between cell-surface-anchored human ACE2 and recombinant SARS-CoV-2 receptor-binding domain (RBD).

Figure 5—figure supplement 1.

Human-ACE2-expressing HEK293T cells were incubated with recombinant His-tagged SARS-CoV-2 RBD (containing either Lys417 or Val417) or buffer only. A fluorescence-labeled anti-His-tag antibody was used to detect cell-bound RBD. The histogram displays the differential fluorescence intensity, indicating the interactions between one of the RBDs and cell-surface ACE2. The (-) control represents cells treated with buffer only.