Fig. 3: Receptor interaction of JN.1, KP.2, KP.3 and KP.3.1.1 spike.
a Cryo-EM structure of the KP.2 spike in complex with ACE2. Two perpendicular views of KP.2 spike-ACE2 are depicted as surface, with ACE2 in dodger blue and the trimeric spike in pink, medium purple, and purple. b Structure of KP.2 RBD-ACE2. c Detailed interactions between the JN.1 spikeF456, Q493-ACE2 (PDB: 8YZD) and the local cryo-EM maps. d Detailed interactions between the KP.2 spikeL456, Q493-ACE2, and the local cryo-EM maps. e Detailed interactions between the KP.3 spikeL456, E493-ACE2 (PDB: 9IUP), and the local cryo-EM maps. f Structural superposition of JN.1 (PDB:8Y5J) and KP.3.1.1 spike trimer. JN.1 and KP.3.1.1 are colored red orange and purple. N30, F32, N61 and glycosylation sites are shown as sticks. The red arrow indicates the conformational change of F32 in the structure of KP.3.1.1 spike trimer compared to JN.1. g The local cryo-EM maps of N30, F32, N61 and glycosylation sites in the structure of KP.3.1.1 spike trimer. h Structural superposition of JN.1 (PDB:8Y5J) and KP.3.1.1 spike trimer. JN.1 and KP.3.1.1 are colored red orange and purple. Red dashed circle indicates the interaction region comprising of Y28, F32, Y91, F216 and Y266, which were shown as sticks. i Structural prediction of the binding between NTD specific antibody C1717 or DH1052 and N30 site of SARS-CoV-2 WT or KP.3.1.1 spike protein. j, k Neutralization curve and IC50 heatmap of selected mAbs against KP.3 and KP.3.1.1 pseudoviruses, as well as their N30A mutant variants (n = 3). The n number represents biological repeats. Data represent mean ± SEM. Data were obtained from three independent experiments. Source data are provided as a Source Data file.
