Evidence map›Paper›PMID 24802048›Full record

ArticlemAbs

Characterization and screening of IgG binding to the neonatal Fc receptor.

Tobias Neuber, Katrin Frese, Jan Jaehrling, Sebastian Jäger, Daniela Daubert, Karin Felderer, Mechthild Linnemann, Anne Höhne, Stefan Kaden, Johanna Kölln and 4 more

Open access · goldAbstract 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 73 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed, 1 pooled it
7.5field-weighted citation impact, top 3% of its field
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

73 citing papers in PubMed, 1 synthesis or guideline pooled it, 106 citations in OpenAlex.

  1. FcRn as a Transporter for Nasal Delivery of Biologics: A Systematic Review.International journal of molecular sciences · 2021
    Pooled it
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  18. Antigen specificity shapes antibody functions in tuberculosis.bioRxiv : the preprint server for biology · 2024
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  20. Article

13 more citing papers are in PubMed but not listed here.

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

14 authors at 2 institutions in 1 country.

Tobias NeuberMorphoSys AG; Martinsried/Planegg, Germany.
Katrin FreseMorphoSys AG; Martinsried/Planegg, Germany.
Jan JaehrlingMorphoSys AG; Martinsried/Planegg, Germany.
Sebastian JägerMorphoSys AG; Martinsried/Planegg, Germany.
Daniela DaubertMorphoSys AG; Martinsried/Planegg, Germany.
Karin FeldererMorphoSys AG; Martinsried/Planegg, Germany.
Mechthild LinnemannMorphoSys AG; Martinsried/Planegg, Germany.
Anne HöhneMorphoSys AG; Martinsried/Planegg, Germany.
Stefan KadenMorphoSys AG; Martinsried/Planegg, Germany.
Johanna KöllnMorphoSys AG; Martinsried/Planegg, Germany.
Thomas TillerMorphoSys AG; Martinsried/Planegg, Germany.
Bodo BrocksMorphoSys AG; Martinsried/Planegg, Germany.
Ralf OstendorpMorphoSys AG; Martinsried/Planegg, Germany.
Stefan PabstMorphoSys AG; Martinsried/Planegg, Germany.
MorphoSys (Germany) · DEUrologische Klinik München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The neonatal Fc receptor (FcRn) protects immunoglobulin G (IgG) from degradation and increases the serum half-life of IgG, thereby contributing to a higher concentration of IgG in the serum. Because altered FcRn binding may result in a reduced or prolonged half-life of IgG molecules, it is advisable to characterize Fc receptor binding of therapeutic antibody lead candidates prior to the start of pre-clinical and clinical studies. In this study, we characterized the interactions between FcRn of different species (human, cynomolgus monkey, mouse and rat) and nine IgG molecules from different species and isotypes with common variable heavy (VH) and variable light chain (VL) domains. Binding was analyzed at acidic and neutral pH using surface plasmon resonance (SPR) and biolayer interferometry (BLI). Furthermore, we transferred the well-accepted, but low throughput SPR-based method for FcRn binding characterization to the BLI-based Octet platform to enable a higher sample throughput allowing the characterization of FcRn binding already during early drug discovery phase. We showed that the BLI-based approach is fit-for-purpose and capable of discriminating between IgG molecules with significant differences in FcRn binding affinities. Using this high-throughput approach we investigated FcRn binding of 36 IgG molecules that represented all VH/VL region combinations available in the fully human, recombinant antibody library Ylanthia®. Our results clearly showed normal FcRn binding profiles for all samples. Hence, the variations among the framework parts, complementarity-determining region (CDR) 1 and CDR2 of the fragment antigen binding (Fab) domain did not significantly change FcRn binding.

Indexed as

AnimalsAntibodies, MonoclonalCell LineComplementarity Determining RegionsHistocompatibility Antigens Class IHumansImmunoglobulin GImmunoglobulin Heavy ChainsImmunoglobulin Light ChainsMacaca fascicularisMiceProtein BindingRatsReceptors, FcRecombinant ProteinsAntibodies, MonoclonalComplementarity Determining RegionsFc receptor, neonatalHistocompatibility Antigens Class IImmunoglobulin GImmunoglobulin Heavy ChainsImmunoglobulin Light ChainsReceptors, FcRecombinant Proteinsbiolayer interferometryequilibrium dissociation constantmonoclonal antibodyneonatal Fc receptorpH dependent bindingsurface plasmon resonanceYlanthia®

Identifiers

PMID24802048
PMCPMC4171027
OpenAlexW1978679376

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.