Evidence map›Paper›PMID 36775946›Full record

ArticleProtein science : a publication of the Protein Society2023

NKp46-specific single domain antibodies enable facile engineering of various potent NK cell engager formats.

Britta Lipinski, Paul Arras, Lukas Pekar, Daniel Klewinghaus, Ammelie Svea Boje, Simon Krah, Jasmin Zimmermann, Katja Klausz, Matthias Peipp, Vanessa Siegmund and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

18 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
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  7. Enhancing NK cell-mediated tumor killing of B7-H6Molecular therapy. Oncology · 2025
    Article
  8. Article
  9. Article
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  11. An engineered NKp46 antibody for construction of multi-specific NK cell engagers.Protein engineering, design & selection : PEDS · 2024
    Article
  12. Review
  13. Article
  14. Article
  15. Article
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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 at 2 institutions in 1 country.

Britta LipinskiProtein Engineering and Antibody Technologies, Merck Healthcare KGaA, Darmstadt, Germany.
Paul ArrasProtein Engineering and Antibody Technologies, Merck Healthcare KGaA, Darmstadt, Germany.
Lukas PekarProtein Engineering and Antibody Technologies, Merck Healthcare KGaA, Darmstadt, Germany.
Daniel KlewinghausProtein Engineering and Antibody Technologies, Merck Healthcare KGaA, Darmstadt, Germany.
Ammelie Svea BojeDivision of Antibody-Based Immunotherapy, Department of Internal Medicine II, University Hospital Schleswig-Holstein and Christian-Albrechts-University Kiel, Kiel, Germany.
Simon KrahProtein Engineering and Antibody Technologies, Merck Healthcare KGaA, Darmstadt, Germany.
Jasmin ZimmermannProtein Engineering and Antibody Technologies, Merck Healthcare KGaA, Darmstadt, Germany.
Katja KlauszDivision of Antibody-Based Immunotherapy, Department of Internal Medicine II, University Hospital Schleswig-Holstein and Christian-Albrechts-University Kiel, Kiel, Germany.
Matthias PeippDivision of Antibody-Based Immunotherapy, Department of Internal Medicine II, University Hospital Schleswig-Holstein and Christian-Albrechts-University Kiel, Kiel, Germany.
Vanessa SiegmundProtein and Cell Sciences, Merck Healthcare KGaA, Darmstadt, Germany.
Andreas EversComputational Chemistry and Biology, Merck Healthcare KGaA, Darmstadt, Germany.
Stefan ZielonkaProtein Engineering and Antibody Technologies, Merck Healthcare KGaA, Darmstadt, Germany.ORCID 0000-0002-4649-2843
Merck (Germany) · DEChristian-Albrechts-Universität zu Kiel · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Herein, we describe the generation of potent NK cell engagers (NKCEs) based on single domain antibodies (sdAbs) specific for NKp46 harboring the humanized Fab version of Cetuximab for tumor targeting. After immunization of camelids, a plethora of different VHH domains were retrieved by yeast surface display. Upon reformatting into Fc effector-silenced NKCEs targeting NKp46 and EGFR in a strictly monovalent fashion, the resulting bispecific antibodies elicited potent NK cell-mediated killing of EGFR-overexpressing tumor cells with potencies (EC

Indexed as

Antibodies, BispecificNeoplasmsSingle-Domain AntibodiesCell Line, TumorErbB ReceptorsHumansKiller Cells, NaturalAntibodies, BispecificErbB ReceptorsSingle-Domain AntibodiesADCCantibody engineeringbispecific antibodymultifunctional antibodyNK cell engagerNK cell redirectionNKp46single domain antibodyvalenciesVHH

Identifiers

PMID36775946
PMCPMC9951198
OpenAlexW4320495093

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.