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<p>Antibody binding affinity and kinetics and antibody binding competition.</p>
Ayush Upadhyay (25157573)
Jeffrey Seow (9415776)
Yilmaz Alguel (24840073)
Joseph Newman (5638340)
Nazia Thakur (9904162)
Abigail L. Hay (25157576)
Jerry C. H. Tam (13955938)
Andrea Nans (5176226)
Richard J. Orton (7832015)
Dalan Bailey (193037)
Peter Cherepanov (369)
Katie J. Doores (346210)
Biophysics
Microbiology
Evolutionary Biology
Ecology
Immunology
Biological Sciences not elsewhere classified
Hematology
Infectious Diseases
Virology
v1wt_06 contact residues
therapeutic antibody development
reactive monoclonal antibodies
mab v1wt_06 binds
increasing spillover potential
human population presents
heavy chain alone
future therapeutic use
confer broad sarbecovirus
circulating viruses suggesting
2 variant neutralisation
2 variants
xlink ">
virus entry
urgent need
rationale design
rational design
neutralising epitopes
including xec
ideal candidates
highly conserved
functionally constrained
discover cross
differing angles
continuing evolution
ace2 competition
<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. 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). The data underlying this Figure can be found in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003882#pbio.3003882.s010" target="_blank">S1 Data</a>.</p> <p>(TIF)</p>
2026-10-01T17:40:02Z
Image
Figure
10.1371/journal.pbio.3003882.s001
https://figshare.com/articles/figure/_p_Antibody_binding_affinity_and_kinetics_and_antibody_binding_competition_p_/34047311
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