ArticleOncotarget2014
A FcγRIII-engaging bispecific antibody expands the range of HER2-expressing breast tumors eligible to antibody therapy.
Article in Oncotarget, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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.
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.
Who cites it
31 citing papers in PubMed, 46 citations in OpenAlex.
- Celldetective, an AI-enhanced image analysis tool for unraveling dynamic cell interactions.eLife · 2026Article
- Development of potent Affitin-based bispecific NK cell engagers for the therapy of MSLN-expressing cancers.Molecular therapy. Oncology · 2025Article
- Advances in augmenting infiltration of active natural killer cells into pediatric and adult solid tumors.Molecular therapy. Oncology · 2025Review
- Antitumor activities against breast cancers by an afucosylated anti-HER2 monoclonal antibody HCancer science · 2024Article
- Combining DNA scaffolds and acoustic force spectroscopy to characterize individual protein bonds.Biophysical journal · 2023Article
- Review
- Bispecific antibodies revolutionizing breast cancer treatment: a comprehensive overview.Frontiers in immunology · 2023Review
- Article
- Anti-NKG2D single domain-based antibodies for the modulation of anti-tumor immune response.Oncoimmunology · 2020Article
- Mesoscale computational protocols for the design of highly cooperative bivalent macromolecules.Scientific reports · 2020Article
- Nanobodies: Next Generation of Cancer Diagnostics and Therapeutics.Frontiers in oncology · 2020Review
- Nanobody-CD16 Catch Bond Reveals NK Cell Mechanosensitivity.Biophysical journal · 2019Article
- Nanobody Engineering: Toward Next Generation Immunotherapies and Immunoimaging of Cancer.Antibodies (Basel, Switzerland) · 2019Review
- Overcoming Resistance to Natural Killer Cell Based Immunotherapies for Solid Tumors.Frontiers in oncology · 2019Review
- A Bispecific Antibody-Based Approach for Targeting Mesothelin in Triple Negative Breast Cancer.Frontiers in immunology · 2019Article
- Theranostics in immuno-oncology using nanobody derivatives.Theranostics · 2019Review
- Selective Engagement of FcγRIV by a M2e-Specific Single Domain Antibody Construct Protects Against Influenza A Virus Infection.Frontiers in immunology · 2019Article
- Influence of the Tumor Microenvironment on NK Cell Function in Solid Tumors.Frontiers in immunology · 2019Review
- Tumor immunotherapy: New aspects of natural killer cells.Chinese journal of cancer research = Chung-kuo yen cheng yen chiu · 2018Article
- One-domain CD4 Fused to Human Anti-CD16 Antibody Domain Mediates Effective Killing of HIV-1-Infected Cells.Scientific reports · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Trastuzumab is established as treatment of HER2high metastatic breast cancers but many limitations impair its efficacy. Here, we report the design of a Fab-like bispecific antibody (HER2bsFab) that displays a moderate affinity for HER2 and a unique, specific and high affinity for FcγRIII. In vitro characterization showed that ADCC was the major mechanism of action of HER2bsFab as no significant HER2-driven effect was observed. HER2bsFab mediated ADCC at picomolar concentration against HER2high, HER2low as well as trastuzumab-refractive cell lines. In vivo HER2bsFab potently inhibited HER2high tumor growth by recruitment of mouse FcγRIII and IV-positive resident effector cells and more importantly, exhibited a net superiority over trastuzumab at inhibiting HER2low tumor growth. Moreover, FcγRIIIA-engagement by HER2bsFab was independent of V/F158 polymorphism and induced a stronger NK cells activation in response to target cell recognition. Thus, taking advantage of its epitope specificity and affinity for HER2 and FcγRIIIA, HER2bsFab exhibits potent anti-tumor activity against HER2low tumors while evading most of trastuzumab Fc-linked limitations thereby potentially enlarging the number of patients eligible for breast cancer immunotherapy.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.