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oai:figshare.com:article/34048936 2026-10-01T17:40:23Z category_1 category_8 category_24 category_39 category_46 category_734 category_128 category_132 category_134 portal_5 item_type_1 month_year_10_2026

V1WT_06 binds to the RBD site V epitope using the heavy chain alone. 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 A) A closeup view of the superimposed structure of V1WT_06 bound to WIV-1 RBD on a trimeric spike (from PDB: 8WLZ). A clash with NTD of chain B is observed when V1WT_06 Fab-RBD complex is aligned onto RBD in the up conformation (chain A) in trimeric WIV-1 spike protein. Notably, the binding site is inaccessible in the RBD-down conformation. B) V1WT_06 heavy chain only interaction with WIV-1 RBD (grey). Heavy and light chains are shown with the dark and light blue ribbons, respectively. C) V1WT_06 epitope footprint overlayed with epitope footprints of other site V neutralising antibodies including S2H97, CC25.4, 5817, R1-32, and E465 patch [<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003882#pbio.3003882.ref017" target="_blank">17</a>,<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003882#pbio.3003882.ref027" target="_blank">27</a>–<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003882#pbio.3003882.ref029" target="_blank">29</a>,<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003882#pbio.3003882.ref035" target="_blank">35</a>]. SARS-CoV-2 RBD (from PDB: 6m0j) is coloured based on the amino acid conservation across 87 bat sarbecoviruses [<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003882#pbio.3003882.ref006" target="_blank">6</a>,<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003882#pbio.3003882.ref023" target="_blank">23</a>,<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003882#pbio.3003882.ref081" target="_blank">81</a>,<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003882#pbio.3003882.ref082" target="_blank">82</a>]. D) Sequence alignment of a panel of bat sarbecovirus RBDs. Contact residues of V1WT_06 mAb on the WIV-1-RBD are indicated with black dots. The colouring scheme describes the percent identity (PID) between the sequences as implemented in Jalview 2.11.4.0. E) Comparison in neutralisation potency of V1WT_06 Fab and IgG against SARS-CoV-2 (D614G), SARS-CoV-1, and WIV-1. Mean values are plotted with error bars showing ± standard deviation (s.d.). 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>. 2026-10-01T17:40:02Z Image Figure 10.1371/journal.pbio.3003882.g002 https://figshare.com/articles/figure/_p_V1WT_06_binds_to_the_RBD_site_V_epitope_using_the_heavy_chain_alone_p_/34048936 CC BY 4.0