Fig. 7: Interactions and interface comparison between SARS-CoV-2 BA.2.86-RBD and JN.1-RBD with ACE2. | Nature Communications

Fig. 7: Interactions and interface comparison between SARS-CoV-2 BA.2.86-RBD and JN.1-RBD with ACE2.

From: Structural basis for the evolution and antibody evasion of SARS-CoV-2 BA.2.86 and JN.1 subvariants

Fig. 7

a Cryo-EM density of the JN.1-RBD–ACE2 interface. The JN.1 RBD is shown in cyan. The ACE2 is shown in salmon. This is an overall cryo-EM density of the RBD–ACE2 region. b The cryo-EM structural alignment of JN.1 and BA.2.86 between the RBD and ACE2 interface. Residues are shown in sticks, with the corresponding cryo-EM density represented in mesh. The BA.2.86 RBD is shown in medium purple. c Detailed analysis of 455 site in JN.1 or BA.2.86 RBD–ACE2-bound region. The region illustrates the disappearance of hydrophobic interactions at 455 site. L455S generates the hydrogen bond interaction with Gln493 in intra-RBD. Polar interactions are indicated by yellow dotted lines. d Detailed analysis of the same interacting residues between RBD and ACE2. The region displays the variation in interaction bond lengths between JN.1 and BA.2.86 at the same interacting residue positions. Polar interactions are indicated by yellow dotted lines. e Detailed analysis of the different interacting residues between RBD and ACE2. The region shows the interacting residues altered in JN.1 compared to BA.2.86. Polar interactions are indicated by yellow dotted lines.

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