Evidence map›Paper›PMID 20418662›Full record

ArticlemAbs

Structural and functional characterization of the trifunctional antibody catumaxomab.

Dirk Chelius, Peter Ruf, Patrick Gruber, Matthias Plöscher, Reinhard Liedtke, Eva Gansberger, Juergen Hess, Michael Wasiliu, Horst Lindhofer

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 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
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

71 citing papers in PubMed, 141 citations in OpenAlex.

  1. Trial
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  8. Immunotherapy for precision medicine in colorectal cancer.Expert review of precision medicine and drug development · 2025
    Article
  9. Review
  10. Advances in the treatment of malignant ascites in China.Supportive care in cancer : official journal of the Multinational Association of Supportive Care in Cancer · 2024
    Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. [Consideration on the Research and Development of Anti-tumor Bispecific Antibody Drugs].Zhongguo fei ai za zhi = Chinese journal of lung cancer · 2022
    Article
  16. Review
  17. Article
  18. Article
  19. Emerging new therapeutic antibody derivatives for cancer treatment.Signal transduction and targeted therapy · 2022
    Review
  20. Review

11 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

9 authors at 1 institution in 1 country.

Dirk CheliusTRION Pharma GmbH, Munich, Germany. dirk.chelius@trionpharma.de
Peter Ruf
Patrick Gruber
Matthias Plöscher
Reinhard Liedtke
Eva Gansberger
Juergen Hess
Michael Wasiliu
Horst Lindhofer
Pharmalog (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Triomab family of trifunctional, bispecific antibodies that maintain an IgG-like shape are novel tumor targeting agents. These chimeras consist of two half antibodies, each with one light and one heavy chain, that originate from parental mouse IgG2a and rat IgG2b isotypes. This combination allows cost-effective biopharmaceutical manufacturing at an industrial scale since this specific mouse/rat isotype combination favors matching of corresponding antibody halves during production by means of quadroma technology. Whereas every Triomab family member is composed of an anti-CD3 rat IgG2b half antibody for T cell recognition, the antigen binding site presented by the mouse IgG2a isotype is exchangeable. Several Triomab antibodies have been generated that bind to tumor-associated antigens, e.g., EpCAM (catumaxomab), HER2/neu (ertumaxomab), CD20 (FBTA05), gangliosides GD2/GD3 (Ektomun), on appropriate tumor target cells associated with carcinomas, lymphomas or melanomas. Catumaxomab (Removab) was launched in Europe for treatment of malignant ascites in April 2009. Here, we report the structural and functional characterization of this product. Mass spectrometry revealed an intact mass of 150511 Dalton (Da) and 23717 Da, 24716 Da, 51957 Da and 52019 Da of the reduced and alkylated rat light chain, mouse light chain, rat heavy chain, mouse heavy chain chains, respectively. The observed masses were in agreement with the expected masses based on the amino acid sequence obtained from cDNA sequencing. The glycosylation profile was similar to other human IgG consisting of biantennary oligosaccharides with different numbers of terminal galactose. CD spectroscopy showed mainly beta-sheets secondary structure that is typical for IgG antibodies. Binding measurement revealed the unique trifunctional features of catumaxomab. Other analytical tools were used to evaluate characteristics of catumaxomab preparations, including the presence of isoforms and aggregates.

Indexed as

AnimalsAntibodies, BispecificCell Line, TumorCytotoxicity, ImmunologicHumansImmunoglobulin Heavy ChainsImmunoglobulin Light ChainsMiceMolecular WeightRatsAntibodies, BispecificcatumaxomabImmunoglobulin Heavy ChainsImmunoglobulin Light Chains

Identifiers

PMID20418662
PMCPMC2881257
OpenAlexW1972193434

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.