Evidence map›Paper›PMID 41220943›Full record

ArticleFrontiers in oncology2025

Engineered multifunctional transforming growth factor-β type II receptor ectodomain fusions for oncology applications.

Anne E G Lenferink, John C Zwaagstra, Jason Baardsnes, Laurence Delafosse, Marie Parat, Umar Iqbal, Etienne Lessard, Arsalan S Haqqani, Anna Jezierski, Afnan Abu-Thuraia and 3 more

Abstract read
In one paragraph

Article in Frontiers in oncology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

13 authors.

Anne E G LenferinkMedical Devices Research Centre, National Research Council Canada, Montréal, QC, Canada.
John C ZwaagstraHuman Health Therapeutics Research Centre, National Research Council Canada, Montréal, QC, Canada.
Jason BaardsnesHuman Health Therapeutics Research Centre, National Research Council Canada, Montréal, QC, Canada.
Laurence DelafosseHuman Health Therapeutics Research Centre, National Research Council Canada, Montréal, QC, Canada.
Marie ParatHuman Health Therapeutics Research Centre, National Research Council Canada, Montréal, QC, Canada.
Umar IqbalHuman Health Therapeutics Research Centre, National Research Council Canada, Ottawa, ON, Canada.
Etienne LessardHuman Health Therapeutics Research Centre, National Research Council Canada, Montréal, QC, Canada.
Arsalan S HaqqaniHuman Health Therapeutics Research Centre, National Research Council Canada, Ottawa, ON, Canada.
Anna JezierskiHuman Health Therapeutics Research Centre, National Research Council Canada, Ottawa, ON, Canada.
Afnan Abu-ThuraiaDepartment of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, ON, Canada.
Sébastien TabarièsDepartment of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, ON, Canada.
Peter M SiegelDepartment of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, ON, Canada.
Traian SuleaHuman Health Therapeutics Research Centre, National Research Council Canada, Montréal, QC, Canada.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Introduction: The transforming growth factor-β (TGF-β) superfamily consists of a large number of evolutionarily conserved and structurally related polypeptide growth factors. TGF-β elicits a wide range of context-dependent cellular responses that play important roles in the maintenance of normal physiological processes and is implicated in various pathologies, including cancer. In healthy cells and in the early stages of cancer development, TGF-β acts as a tumor suppressor by inducing cell cycle arrest and apoptosis. However, in late-stage cancer cells, TGF-β can promote tumorigenesis, including epithelial-mesenchymal transition (EMT), metastasis and chemoresistance. Methods: The dual-function and pleiotropic nature of TGF-β makes therapeutic targeting of this molecule a significant challenge. In this report, we describe the design and development of a novel class of TGF-β-targeting therapeutics in which the TGF-β type II receptor ectodomain (TβRII-ED) can be fused to an intact antibody, such as Cetuximab, or an antibody Fc fragment, without compromising the TβRII-ED or antibody function. Results and Discussion: As such, we constructed and characterized specific TβRII-ED-Fc fusions that act as efficient TGF-β ligand traps with picomolar in vitro neutralizing potencies against TGF-β1 and TGF-β3 isoforms, but not TGF-β2. We further demonstrate that TβRII-ED-Fc is a versatile ligand-trapping module that, when combined with a specific targeting moiety, can lead to powerful anticancer biotherapeutics targeted to and retained at the tumor site, by efficiently neutralizing the tumor-promoting activities of TGF-β

Indexed as

blood-brain barrierbone tumor microenvironmentepithelial-mesenchymal transitionFc-fragment fusionligand traptargeted therapytransforming growth factor β

Identifiers

PMID41220943
PMCPMC12597760

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Registered trials

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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.