Fig. 3: Antigenic landscape of SARS-CoV-2 N reveals at least seven antigenic sites distributed across all domains of the protein. | Nature Communications

Fig. 3: Antigenic landscape of SARS-CoV-2 N reveals at least seven antigenic sites distributed across all domains of the protein.

From: Structural stabilization of the intrinsically disordered SARS-CoV-2 N by binding to RNA sequences engineered from the viral genome fragment

Fig. 3

A Mice immunization with purified recombinant N and isolation of a panel of 88 novel mAbs using a single B cell-sorting Beacon platform. B Number of novel high-affinity mAbs distributed across the rigid and the disordered domains of N protein. A, B Created in BioRender. Saphire, E. (2025) https://BioRender.com/6guzz6f. C Above: Phylogenetic tree based on the variable region sequence of the anti-N mAbs. Below: Heat map of mAb binding profile measured by ELISA. Binding domain across N protein and the epitope group of each mAb is indicated. D Iso-affinity kinetic plot (association vs. dissociation constant) grouped by mAb. E Epitope binning clusters (Carterra LSA platform) for the selected mAbs. Two independent antibody binding sites in RNA-BD (RNA-BD I and RNA-BD II) and other two in the DD (DD I and DD II) were identified. 2D class averages illustrate the presence of two independent antibody binding sites in each rigid domain of N. The mAbs NP1-E2 and NP3-D1 were used to complex the RNA-BD. The mAbs NP3-B4 and NP1-E9 were used to complex the DD. Source data are provided as a Source Data file. F NS-EM reconstructions of the RNA-BD (left) or DD (right) bound to mAbs from non-overlapping epitope groups.

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