Evidence map›Paper›PMID 20309546›Full record

ArticleCancer immunology, immunotherapy : CII2010

Epitope distance to the target cell membrane and antigen size determine the potency of T cell-mediated lysis by BiTE antibodies specific for a large melanoma surface antigen.

Claudia Bluemel, Susanne Hausmann, Petra Fluhr, Mirnalini Sriskandarajah, William B Stallcup, Patrick A Baeuerle, Peter Kufer

Open access · greenAbstract read
In one paragraph

Article in Cancer immunology, immunotherapy : CII, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed, 2 pooled it
3.8field-weighted citation impact, top 6% 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

126 citing papers in PubMed, 2 syntheses or guidelines pooled it, 204 citations in OpenAlex.

  1. T-Cell Engagers TargetingInternational journal of molecular sciences · 2026
    Pooled it
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  12. Solution structure and synaptic analyses reveal determinants of bispecific T cell engager potency.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  14. Enhancing NK cell-mediated tumor killing of B7-H6Molecular therapy. Oncology · 2025
    Article
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  19. Differential roles of kinetic on- and off-rates in T-cell receptor signal integration revealed with a modified Fab'-DNA ligand.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Article

66 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

7 authors at 2 institutions in 2 countries.

Claudia BluemelMicromet AG, Staffelseestr. 2, 81477, Munich, Germany.
Susanne Hausmann
Petra Fluhr
Mirnalini Sriskandarajah
William B Stallcup
Patrick A Baeuerle
Peter Kufer
3D-Micromac (Germany) · DESanford Burnham Prebys Medical Discovery Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Melanoma chondroitin sulfate proteoglycan (MCSP; also called CSPG4, NG2, HMW-MAA, MSK16, MCSPG, MEL-CSPG, or gp240) is a surface antigen frequently expressed on human melanoma cells, which is involved in cell adhesion, invasion and spreading, angiogenesis, complement inhibition, and signaling. MCSP has therefore been frequently selected as target antigen for development of antibody- and vaccine-based therapeutic approaches. We have here used a large panel of monoclonal antibodies against human MCSP for generation of single-chain MCSP/CD3-bispecific antibodies of the BiTE (for bispecific T cell engager) class. Despite similar binding affinity to MCSP, respective BiTE antibodies greatly differed in their potency of redirected lysis of CHO cells stably transfected with full-length human MCSP, or with various MCSP deletion mutants and fusion proteins. BiTE antibodies binding to the membrane proximal domain D3 of MCSP were more potent than those binding to more distal domains. This epitope distance effect was corroborated with EpCAM/CD3-bispecific BiTE antibody MT110 by testing various fusion proteins between MCSP and EpCAM as surface antigens. CHO cells expressing small surface target antigens were generally better lysed than those expressing larger target antigens, indicating that antigen size was also an important determinant for the potency of BiTE antibody. The present study for the first time relates the positioning of binding domains and size of surface antigens to the potency of target cell lysis by BiTE-redirected cytotoxic T cells. In case of the MCSP antigen, this provides the basis for selection of a maximally potent BiTE antibody candidate for development of a novel melanoma therapy.

Indexed as

Cancer VaccinesAnimalsAntibodies, BispecificAntigens, NeoplasmCD3 ComplexCHO CellsChondroitin Sulfate Proteoglycan 4Chondroitin Sulfate ProteoglycansCricetinaeCricetulusCytotoxicity, ImmunologicEpitopes, T-LymphocyteHumansMelanomaMembrane ProteinsProtein BindingAntibodies, BispecificAntigens, NeoplasmCancer VaccinesCD3 ComplexChondroitin Sulfate Proteoglycan 4Chondroitin Sulfate ProteoglycansCSPG4 protein, humanEpitopes, T-LymphocyteMembrane ProteinsRecombinant Fusion ProteinsSingle-Chain Antibodies

Identifiers

PMID20309546
PMCPMC11030089
OpenAlexW2055342376

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.