Evidence map›Paper›PMID 40628825›Full record

ArticleScientific reports2025

Anti-IgD nanobodies as novel tools for studying human IgD biology.

Susan K Vester, Rebecca L Beavil, Alexander Alexandrovich, Hannah J Gould, Andrew J Beavil, Brian J Sutton, James M McDonnell

Abstract read
In one paragraph

Article in Scientific reports, 2025. 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

7 authors.

Susan K VesterRandall Centre for Cell and Molecular Biophysics, King's College London, New Hunt's House, London, SE1 1UL, UK.
Rebecca L BeavilRandall Centre for Cell and Molecular Biophysics, King's College London, New Hunt's House, London, SE1 1UL, UK.
Alexander AlexandrovichRandall Centre for Cell and Molecular Biophysics, King's College London, New Hunt's House, London, SE1 1UL, UK.
Hannah J GouldRandall Centre for Cell and Molecular Biophysics, King's College London, New Hunt's House, London, SE1 1UL, UK.
Andrew J BeavilRandall Centre for Cell and Molecular Biophysics, King's College London, New Hunt's House, London, SE1 1UL, UK.
Brian J SuttonRandall Centre for Cell and Molecular Biophysics, King's College London, New Hunt's House, London, SE1 1UL, UK.
James M McDonnellRandall Centre for Cell and Molecular Biophysics, King's College London, New Hunt's House, London, SE1 1UL, UK. james.mcdonnell@kcl.ac.uk.

Funding

Medical Research Council MR/V010557/1Wellcome Trust
6 · The paper itself

Abstract

IgD is the least well characterized of mammalian antibody isotypes and its biology remains poorly understood. Nanobodies are a useful and versatile tool for research and diagnostics, including for protein purification, capture and detection applications. Here we report the characterization of four anti-human IgD nanobodies, specific to the Fc region of IgD. The four nanobodies bound to human IgD with low nanomolar affinity, showing different binding kinetics and interaction stoichiometries, as well as recognizing four distinct epitopes. We found one of these anti-IgD nanobodies, aδNb408, to be an excellent purification tool for IgD, with efficient capture and elution at pH 3.5. To aid the analysis of IgD interactions using surface plasmon resonance, we identified two nanobodies that provided good capture of IgD. Assembling bispecific and bivalent nanobody pairs increased the avidity of the anti-IgD nanobodies, with the bispecific nanobody pair aδNb408-aδNb107 showing robust detection of IgD on Namalwa B cells. The anti-IgD nanobody tools described here can be used for diverse applications that have the potential to further our understanding of IgD biology.

Indexed as

Immunoglobulin DSingle-Domain AntibodiesAntibodies, BispecificAntibody AffinityB-LymphocytesEpitopesHumansProtein BindingSurface Plasmon ResonanceAntibodies, BispecificEpitopesImmunoglobulin DSingle-Domain AntibodiesAntibodyBispecificFcImmunoglobulin D (IgD)NanobodySurface plasmon resonance

Identifiers

PMID40628825
PMCPMC12238353

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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.