Evidence map›Paper›PMID 32887531›Full record

ArticlemAbs

Biophysical and biochemical characterization of a VHH-based IgG-like bi- and trispecific antibody platform.

Lukas Pekar, Michael Busch, Bernhard Valldorf, Steffen C Hinz, Lars Toleikis, Simon Krah, Stefan Zielonka

Abstract readVideo-Audio Media
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 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Fully synthetic platform to rapidly generate tetravalent bispecific nanobody-based immunoglobulins.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Application Progress of the Single Domain Antibody in Medicine.International journal of molecular sciences · 2023
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

7 authors.

Lukas PekarInstitute for Organic Chemistry and Biochemistry , Technische Universität Darmstadt, Darmstadt, Germany.
Michael BuschDiscovery Pharmacology, Merck KGaA , Darmstadt, Germany.
Bernhard ValldorfChemical and Pharmaceutical Development, Merck KGaA , Darmstadt, Germany.
Steffen C HinzInstitute for Organic Chemistry and Biochemistry , Technische Universität Darmstadt, Darmstadt, Germany.
Lars ToleikisProtein Engineering and Antibody Technologies, Merck KGaA , Darmstadt, Germany.
Simon KrahProtein Engineering and Antibody Technologies, Merck KGaA , Darmstadt, Germany.
Stefan ZielonkaProtein Engineering and Antibody Technologies, Merck KGaA , Darmstadt, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Here, we report the characterization of a VHH-derived IgG-like bi- and trispecific antibody platform that essentially relies on the replacement of the VH and VL regions of a conventional antibody by two independently functioning VHH domains. Consequently, a VHH is engrafted onto constant region CH1 while the other VHH-based paratope is engrafted on the constant region of the light chain, Cκ or Cλ, resulting in a tetravalent bispecific IgG-like molecule. Combined with a heavy chain heterodimerization technique, this platform allows facile engineering of bi- and trispecific antibodies with flexible valencies. We demonstrate the general applicability of this generic platform approach and elaborate on the limitations of specific formats.

Indexed as

Antibodies, BispecificImmunoglobulin GImmunoglobulin Heavy ChainsImmunoglobulin Variable RegionCell Line, TumorHumansAntibodies, BispecificImmunoglobulin GImmunoglobulin Heavy ChainsImmunoglobulin Variable RegionAntibody engineeringbispecific antibodycamelidIgG-likenanobodysingle-domain antibodytrispecific antibodyVHH

Identifiers

PMID32887531
PMCPMC7531565

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.