Evidence map›Paper›PMID 33448242›Full record

ArticlemAbs

Ab-Ligity: identifying sequence-dissimilar antibodies that bind to the same epitope.

Wing Ki Wong, Sarah A Robinson, Alexander Bujotzek, Guy Georges, Alan P Lewis, Jiye Shi, James Snowden, Bruck Taddese, Charlotte M Deane

Abstract read
In one paragraph

Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. AI-Driven BCR Modeling for Precision Immunology.International journal of molecular sciences · 2026
    Review
  2. Article
  3. Article
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  5. Review
  6. Article
  7. Article
  8. Computational detection of antigen-specific B cell receptors following immunization.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Recent Progress in Antibody Epitope Prediction.Antibodies (Basel, Switzerland) · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Antibodies as drugs-a Keystone Symposia report.Annals of the New York Academy of Sciences · 2023
    Article
  19. Article
  20. Article
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

9 authors.

Wing Ki WongDepartment of Statistics, University of Oxford , Oxford, UK.ORCID 0000-0003-4029-6902
Sarah A RobinsonDepartment of Statistics, University of Oxford , Oxford, UK.ORCID 0000-0003-2500-0173
Alexander BujotzekRoche Pharma Research and Early Development, Large Molecule Research, Roche Innovation Center Munich , Penzberg, Germany.
Guy GeorgesRoche Pharma Research and Early Development, Large Molecule Research, Roche Innovation Center Munich , Penzberg, Germany.ORCID 0000-0001-5737-006X
Alan P LewisData and Computational Sciences, GlaxoSmithKline Research and Development , Stevenage, UK.
Jiye ShiUCB Pharma , Slough, UK.ORCID 0000-0002-9628-8680
James SnowdenUCB Pharma , Slough, UK.
Bruck TaddeseDiscovery Sciences, BioPharmaceuticals, R&D, AstraZeneca , Cambridge, UK.
Charlotte M DeaneDepartment of Statistics, University of Oxford , Oxford, UK.ORCID 0000-0003-1388-2252

Funding

Medical Research Council EP/L016044/1
6 · The paper itself

Abstract

Solving the structure of an antibody-antigen complex gives atomic level information of the interactions between an antibody and its antigen, but such structures are expensive and hard to obtain. Alternative experimental sources include epitope mapping and binning experiments, which can be used as a surrogate to identify key interacting residues. However, their resolution is usually not sufficient to identify if two antibodies have identical interactions. Computational approaches to this problem have so far been based on the premise that antibodies with similar sequences behave similarly. Such approaches will fail to identify sequence-distant antibodies that target the same epitope. Here, we present Ab-Ligity, a structure-based similarity measure tailored to antibody-antigen interfaces. Using predicted paratopes on model antibody structures, we assessed its ability to identify those antibodies that target highly similar epitopes. Most antibodies adopting similar binding modes can be identified from sequence similarity alone, using methods such as clonotyping. In the challenging subset of antibodies whose sequences differ significantly, Ab-Ligity is still able to predict antibodies that would bind to highly similar epitopes (precision of 0.95 and recall of 0.69). We compared Ab-Ligity's performance to an existing tool for comparing general protein interfaces, InterComp, and showed improved performance on antibody cases achieved in a substantially reduced time. These results suggest that Ab-Ligity will allow the identification of diverse (sequence-dissimilar) antibodies that bind to the same epitopes from large datasets such as immune repertoires. The tool is available at http://opig.stats.ox.ac.uk/resources.

Indexed as

AlgorithmsAntibodiesAntigen-Antibody ComplexAntigensBinding Sites, AntibodyComputational BiologyCrystallography, X-RayEpitope MappingEpitopesHumansProtein BindingAntibodiesAntigen-Antibody ComplexAntigensEpitopesAntibodycomparisonparatopestructure

Identifiers

PMID33448242
PMCPMC7833755

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Registered trials

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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.