Evidence map›Paper›PMID 40662295›Full record

ArticlemAbs2025

Trispecific SEED antibodies engineered for neutrophil-mediated cell killing.

Veronica Natale, Gergely Heves, Katharina Stadlbauer, Florian Rüker, Vanessa Siegmund, Lukas Pekar, Stefan Zielonka, Lars Toleikis, Stefan Becker, Gordana Wozniak-Knopp

Abstract read
In one paragraph

Article in mAbs, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. 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

10 authors.

Veronica NataleChristian Doppler Laboratory for Innovative Immunotherapeutics, Institute of Molecular Biotechnology, Department of Biotechnology, University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.ORCID 0000-0003-0317-675X
Gergely HevesChristian Doppler Laboratory for Innovative Immunotherapeutics, Institute of Molecular Biotechnology, Department of Biotechnology, University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.
Katharina StadlbauerChristian Doppler Laboratory for Innovative Immunotherapeutics, Institute of Molecular Biotechnology, Department of Biotechnology, University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.ORCID 0000-0002-0724-5874
Florian RükerChristian Doppler Laboratory for Innovative Immunotherapeutics, Institute of Molecular Biotechnology, Department of Biotechnology, University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.ORCID 0000-0001-7639-2686
Vanessa SiegmundNBE Technologies, Global Research and Development, Merck Healthcare KGaA, Darmstadt, Germany.
Lukas PekarNBE Technologies, Global Research and Development, Merck Healthcare KGaA, Darmstadt, Germany.ORCID 0000-0001-9259-0965
Stefan ZielonkaNBE Technologies, Global Research and Development, Merck Healthcare KGaA, Darmstadt, Germany.ORCID 0000-0002-4649-2843
Lars ToleikisNBE Technologies, Global Research and Development, Merck Healthcare KGaA, Darmstadt, Germany.
Stefan BeckerNBE Technologies, Global Research and Development, Merck Healthcare KGaA, Darmstadt, Germany.ORCID 0009-0008-0246-6804
Gordana Wozniak-KnoppChristian Doppler Laboratory for Innovative Immunotherapeutics, Institute of Molecular Biotechnology, Department of Biotechnology, University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.ORCID 0000-0002-4069-070X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Immunoglobulin (Ig) A has attracted interest as a proposed therapeutic agent due to its ability to engage cell groups differently compared to an IgG scaffold and elicit tumor eradication. Further, its multimeric forms enable increased flexibility in the design of available paratopes. The latter is particularly advantageous for bi- and multispecific antibody formats, which are unparalleled in their enhanced selectivity and unique biological functions. We engineered bispecific heterodimeric IgA-based antibodies using the strand-exchanged engineered domain (SEED) technology, which relies on intertwined segments of IgA and IgG in the C

Indexed as

Antibodies, BispecificAntibody-Dependent Cell CytotoxicityImmunoglobulin ANeutrophilsProtein EngineeringAnimalsAntigens, CDCell Line, TumorHumansReceptors, FcAntibodies, BispecificAntigens, CDFc(alpha) receptorImmunoglobulin AReceptors, FcADCCbispecific antibodyEGFRFc alpha RIimmunoglobulin aneutrophilsROR1strand-exchanged engineered domain (SEED)

Identifiers

PMID40662295
PMCPMC12269659

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.