Evidence map›Paper›PMID 36494671›Full record

ArticleJournal of translational medicine2022

A bispecific, crosslinking lectibody activates cytotoxic T cells and induces cancer cell death.

Francesca Rosato, Rajeev Pasupuleti, Jana Tomisch, Ana Valeria Meléndez, Dajana Kolanovic, Olga N Makshakova, Birgit Wiltschi, Winfried Römer

Open access · goldAbstract read
In one paragraph

Article in Journal of translational medicine, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
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  5. Chimerolectins: Classification, structural architecture, and functional perspectives.Protein science : a publication of the Protein Society · 2025
    Review
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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

8 authors at 3 institutions in 3 countries.

Francesca Rosato *Faculty of Biology, University of Freiburg, Freiburg, Germany.ORCID 0000-0002-9255-9391
Rajeev Pasupuleti *ACIB - The Austrian Centre of Industrial Biotechnology, Graz, Austria.ORCID 0000-0002-9399-2699
Jana TomischFaculty of Biology, University of Freiburg, Freiburg, Germany.ORCID 0000-0002-4656-9345
Ana Valeria MeléndezFaculty of Biology, University of Freiburg, Freiburg, Germany.ORCID 0000-0001-6267-2855
Dajana KolanovicACIB - The Austrian Centre of Industrial Biotechnology, Graz, Austria.ORCID 0000-0002-2536-1182
Olga N MakshakovaFaculty of Biology, University of Freiburg, Freiburg, Germany.ORCID 0000-0002-0615-3513
Birgit WiltschiACIB - The Austrian Centre of Industrial Biotechnology, Graz, Austria. birgit.wiltschi@acib.at.ORCID 0000-0001-5230-0951
Winfried RömerFaculty of Biology, University of Freiburg, Freiburg, Germany. winfried.roemer@bioss.uni-freiburg.de.ORCID 0000-0002-2847-246X
University of Freiburg · DEInstitute of Molecular Biotechnology · ATGraz University of Technology · AT

Funding

Marie Curie 814029
6 · The paper itself

Abstract

backgroundAberrant glycosylation patterns play a crucial role in the development of cancer cells as they promote tumor growth and aggressiveness. Lectins recognize carbohydrate antigens attached to proteins and lipids on cell surfaces and represent potential tools for application in cancer diagnostics and therapy. Among the emerging cancer therapies, immunotherapy has become a promising treatment modality for various hematological and solid malignancies. Here we present an approach to redirect the immune system into fighting cancer by targeting altered glycans at the surface of malignant cells. We developed a so-called "lectibody", a bispecific construct composed of a lectin linked to an antibody fragment. This lectibody is inspired by bispecific T cell engager (BiTEs) antibodies that recruit cytotoxic T lymphocytes (CTLs) while simultaneously binding to tumor-associated antigens (TAAs) on cancer cells. The tumor-related glycosphingolipid globotriaosylceramide (Gb3) represents the target of this proof-of-concept study. It is recognized with high selectivity by the B-subunit of the pathogen-derived Shiga toxin, presenting opportunities for clinical development.

methodsThe lectibody was realized by conjugating an anti-CD3 single-chain antibody fragment to the B-subunit of Shiga toxin to target Gb3

resultsThis proof-of-concept study demonstrates that the lectibody activates T cells for their cytotoxic signaling, redirecting CTLs´ cytotoxicity in a highly selective manner and resulting in nearly complete tumor cell lysis-up to 93%-of Gb3

conclusionsThis research highlights the potential of lectins in targeting certain tumors, with an opportunity for new cancer treatments. When considering a combinatorial strategy, lectin-based platforms of this type offer the possibility to target glycan epitopes on tumor cells and boost the efficacy of current therapies, providing an additional strategy for tumor eradication and improving patient outcomes.

Indexed as

Antibodies, BispecificNeoplasmsCD3 ComplexCell DeathHumansImmunoglobulin FragmentsLectinsLymphocyte ActivationShiga ToxinT-Lymphocytes, CytotoxicAntibodies, BispecificCD3 ComplexImmunoglobulin FragmentsLectinsShiga ToxinBispecific targetingCancer immunotherapyClick chemistryGlobotriaosylceramideLectinsShiga toxinT cellsTumor-associated carbohydrate antigens

Identifiers

PMID36494671
PMCPMC9733292
OpenAlexW4311974457

What OpenQuestion holds

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LicenceCC BY
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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.