2026-10-12T09:27:12Z https://api.figshare.com/v2/oai

oai:figshare.com:article/34048927 2026-10-01T17:40:19Z category_1 category_8 category_24 category_39 category_46 category_734 category_128 category_132 category_134 portal_5 item_type_3 month_year_10_2026

<p>All raw data that supports the figures.</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 <div><p>The continuing evolution of SARS-CoV-2 variants of concern, and the increasing spillover potential of sarbecoviruses into the human population presents an important and urgent need to discover cross-reactive monoclonal antibodies (mAbs) for future therapeutic use and identify conserved neutralising epitopes that can be used for rationale design of broadly protective sarbecovirus vaccines. Here we study the neutralising epitopes on WIV-1 Spike of three mAbs that confer broad sarbecovirus and SARS-CoV-2 variant neutralisation, including XEC, JN.1, and XFG. mAb V1WT_06 binds a highly conserved RBD site V epitope that is mediated by the heavy chain alone. V1WT_06 contact residues are highly conserved in circulating viruses suggesting that the epitope is evolutionarily and functionally constrained. mAbs V1WT_41 and VA14_26 bind overlapping RBD class 4 epitopes with differing angles of approach that impact on the degree of ACE2 competition. We show that neutralisation by these mAbs is maintained when virus entry is via Japanese horseshoe bat and Halcyon horseshoe bat ACE2s. These mAbs are ideal candidates for therapeutic antibody development and inform the rational design of pan-betacoronavirus vaccines.</p></div> 2026-10-01T17:40:02Z Dataset Dataset 10.1371/journal.pbio.3003882.s010 https://figshare.com/articles/dataset/_p_All_raw_data_that_supports_the_figures_p_/34048927 CC BY 4.0