Evidence map›Paper›PMID 42821509›Full record

ArticlePLoS biology2026

Targeting of conserved spike epitopes enables broad antibody neutralisation of diverse bat sarbecoviruses.

Ayush Upadhyay, Jeffrey Seow, Yilmaz Alguel, Joseph Newman, Nazia Thakur, Abigail L Hay, Jerry C H Tam, Andrea Nans, Richard J Orton, Dalan Bailey and 2 more

Abstract read
In one paragraph

Article in PLoS biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Ayush UpadhyayDepartment of Infectious Diseases, School of Immunology & Microbial Sciences, King's College London, London, United Kingdom.
Jeffrey SeowDepartment of Infectious Diseases, School of Immunology & Microbial Sciences, King's College London, London, United Kingdom.
Yilmaz AlguelChromatin Structure and Mobile DNA Laboratory, The Francis Crick Institute, London, United Kingdom.
Joseph NewmanThe Pirbright Institute, Woking, Surrey, United Kingdom.
Nazia ThakurThe Pirbright Institute, Woking, Surrey, United Kingdom.
Abigail L HayThe Pirbright Institute, Woking, Surrey, United Kingdom.
Jerry C H TamDepartment of Infectious Diseases, School of Immunology & Microbial Sciences, King's College London, London, United Kingdom.
Andrea NansStructural Biology Science Technology Platform, The Francis Crick Institute, London, United Kingdom.
Richard J OrtonMRC-University of Glasgow Centre for Virus Research, The University of Glasgow, Glasgow, United Kingdom.
Dalan BaileyThe Pirbright Institute, Woking, Surrey, United Kingdom.
Peter CherepanovChromatin Structure and Mobile DNA Laboratory, The Francis Crick Institute, London, United Kingdom.
Katie J DooresDepartment of Infectious Diseases, School of Immunology & Microbial Sciences, King's College London, London, United Kingdom.ORCID https://orcid.org/0000-0002-5507-1725

Funding

Bill & Melinda Gates Foundation INV-035610Wellcome Trust CC2058
6 · The paper itself

Abstract

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.

Indexed as

Antibodies, NeutralizingAntibodies, ViralChiropteraEpitopesSpike Glycoprotein, CoronavirusAnimalsAntibodies, MonoclonalBetacoronavirusCross ReactionsHumansSARS-CoV-2Antibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitopesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID42821509
PMCPMC13630248

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.