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Data · dataset · 2026

<p>Antibody binding affinity and kinetics and antibody binding competition.</p>

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<p><b>A)</b> Affinity (K<sub>D</sub>), association rate constant (k<sub>a</sub>) and dissociation rate constant (k<sub>d</sub>) of mAb binding kinetics for SARS-CoV-2 RBD were measured by surface plasmon resonance using the Carterra LSA platform.

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Values are coloured in accordance with the gradients presented. <b>B)</b> Binding of mAbs to cell surface expressed Spike by flow cytometry including Clade 1a (Rs4231, WIV-1), Clade 1b (RpYN06) and Clade 2 (RacCS203, RP3/2004, and RF1/2004). <b>C)</b> Each Spike had a C-terminal FLAG-tag and expression of Spike was confirmed by western blot of transfected cell lysates. <b>D)</b> Heatmap of antibody blocking and sandwiching interactions between VA14_26, V1WT_41, and V1WT_06 measured using SPR against SARS-CoV-2 RBD.

Antibodies immobilised as ligands are listed on the left and analytes injected are listed across the top. The scale shows the normalised change in response units (RU) relative to injection of PBS after RBD. RU > 0.3 show sandwiching analytes (i.e., no competition) and RU < 0.3 shows blocked or displaced analytes (i.e., competition).

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The data underlying this Figure can be found in <a href="plosbiology.org/article/info:doi/10.1371/journal.pbio.3003882#pbio.3003882.s010" target="_blank">S1 Data</a>.</p> <p>(TIF)</p>

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