Evidence map›Paper›PMID 34759924›Full record

ArticleFrontiers in immunology2021

Milking the Cow: Cattle-Derived Chimeric Ultralong CDR-H3 Antibodies and Their Engineered CDR-H3-Only Knobbody Counterparts Targeting Epidermal Growth Factor Receptor Elicit Potent NK Cell-Mediated Cytotoxicity.

Lukas Pekar, Daniel Klewinghaus, Paul Arras, Stefania C Carrara, Julia Harwardt, Simon Krah, Desislava Yanakieva, Lars Toleikis, Vaughn V Smider, Harald Kolmar and 1 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Phage Display of Bovine Ultralong CDRH3.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. 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

11 authors at 3 institutions in 2 countries.

Lukas PekarProtein Engineering and Antibody Technologies, Merck Healthcare KGaA, Darmstadt, Germany.
Daniel KlewinghausProtein Engineering and Antibody Technologies, Merck Healthcare KGaA, Darmstadt, Germany.
Paul ArrasProtein Engineering and Antibody Technologies, Merck Healthcare KGaA, Darmstadt, Germany.
Stefania C CarraraInstitute for Organic Chemistry and Biochemistry, Technische Universität Darmstadt, Darmstadt, Germany.
Julia HarwardtInstitute for Organic Chemistry and Biochemistry, Technische Universität Darmstadt, Darmstadt, Germany.
Simon KrahProtein Engineering and Antibody Technologies, Merck Healthcare KGaA, Darmstadt, Germany.
Desislava YanakievaProtein Engineering and Antibody Technologies, Merck Healthcare KGaA, Darmstadt, Germany.
Lars ToleikisProtein Engineering and Antibody Technologies, Merck Healthcare KGaA, Darmstadt, Germany.
Vaughn V SmiderThe Applied Biomedical Science Institute, San Diego, CA, United States.
Harald KolmarInstitute for Organic Chemistry and Biochemistry, Technische Universität Darmstadt, Darmstadt, Germany.
Stefan ZielonkaProtein Engineering and Antibody Technologies, Merck Healthcare KGaA, Darmstadt, Germany.
Merck (Germany) · DETechnical University of Darmstadt · DEScripps Research Institute · US

Funding

Molecular and Structural Studies of Antibody Diversity MechanismsR01GM105826 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SMIDER, VAUGHN VASIL · 2014 to 2021
$3.1M
NIGMS NIH HHS R01 GM105826
6 · The paper itself

Abstract

In this work, we have generated epidermal growth factor receptor (EGFR)-specific cattle-derived ultralong CDR-H3 antibodies by combining cattle immunization with yeast surface display. After immunization, ultralong CDR-H3 regions were specifically amplified and grafted onto an IGHV1-7 scaffold by homologous recombination to facilitate Fab display. Antigen-specific clones were readily obtained by fluorescence-activated cell sorting (FACS) and reformatted as chimeric antibodies. Binning experiments revealed epitope targeting of domains I, II, and IV of EGFR with none of the generated binders competing with Cetuximab, Matuzumab, or EGF for binding to EGFR. Cattle-derived chimeric antibodies were potent in inducing antibody-dependent cell-mediated cytotoxicity (ADCC) against EGFR-overexpressing tumor cells with potencies (EC

Indexed as

AnimalsAntibodiesAntibody AffinityCattleComplementarity Determining RegionsCytotoxicity, ImmunologicErbB ReceptorsHumansKiller Cells, NaturalProtein EngineeringAntibodiesComplementarity Determining RegionsEGFR protein, humanErbB Receptorsantibody displayantibody engineeringcattle antibodyKnobbodyultralong CDR3yeast surface display

Identifiers

PMID34759924
PMCPMC8573386
OpenAlexW3208650261

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.