ArticleFrontiers in immunology2018
Glyco-Engineered Anti-Human Programmed Death-Ligand 1 Antibody Mediates Stronger CD8 T Cell Activation Than Its Normal Glycosylated and Non-Glycosylated Counterparts.
Article in Frontiers in immunology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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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.
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Who cites it
20 citing papers in PubMed, 28 citations in OpenAlex.
- Glycoscience in Advancing PD-1/PD-L1-Axis-Targeted Tumor Immunotherapy.International journal of molecular sciences · 2025Review
- Comprehensive assessment of TECENTRIQ® and OPDIVO®: analyzing immunotherapy indications withdrawn in triple-negative breast cancer and hepatocellular carcinoma.Cancer metastasis reviews · 2024Review
- Glycosylation and Its Role in Immune Checkpoint Proteins: From Molecular Mechanisms to Clinical Implications.Biomedicines · 2024Review
- Design and engineering of bispecific antibodies: insights and practical considerations.Frontiers in bioengineering and biotechnology · 2024Review
- In vitro and in vivo studies of plant-produced Atezolizumab as a potential immunotherapeutic antibody.Scientific reports · 2023Article
- The Role of Clinical Glyco(proteo)mics in Precision Medicine.Molecular & cellular proteomics : MCP · 2023Article
- Controlled release of enhanced cross-hybrid IgGA Fc PD-L1 inhibitors using oncolytic adenoviruses.Molecular therapy oncolytics · 2023Article
- A glycoengineered therapeutic anti-HBV antibody that allows increased HBsAg immunoclearance improves HBV suppressionFrontiers in pharmacology · 2023Article
- Development of a bispecific antibody targeting PD-L1 and TIGIT with optimal cytotoxicity.Scientific reports · 2022Article
- Immobilization-Free Binding and Affinity Characterization of Higher Order Bispecific Antibody Complexes Using Size-Based Microfluidics.Analytical chemistry · 2022Article
- Finding the Right Heavy Chains for Immunostimulatory Antibodies.International journal of molecular sciences · 2022Review
- Immunotherapy in non-small cell lung cancer: Past, present, and future directions.Frontiers in oncology · 2022Review
- Novel oncolytic adenovirus expressing enhanced cross-hybrid IgGA Fc PD-L1 inhibitor activates multiple immune effector populations leading to enhanced tumor killing in vitro, in vivo and with patient-derived tumor organoids.Journal for immunotherapy of cancer · 2021Article
- Recent Findings in the Posttranslational Modifications of PD-L1.Journal of oncology · 2020Review
- Structure and Optimization of Checkpoint Inhibitors.Cancers · 2019Review
- NK Cell-Fc Receptors Advance Tumor Immunotherapy.Journal of clinical medicine · 2019Review
- Review
- The Diverse Contributions of Fucose Linkages in Cancer.Cancers · 2019Review
- FcγR-Binding Is an Important Functional Attribute for Immune Checkpoint Antibodies in Cancer Immunotherapy.Frontiers in immunology · 2019Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The programmed death 1 (PD-1)/programmed death-ligand 1 (PD-L1) axis plays a central role in suppression of anti-tumor immunity. Blocking the axis by targeting PD-L1 with monoclonal antibodies is an effective and already clinically approved approach to treat cancer patients. Glyco-engineering technology can be used to optimize different properties of monoclonal antibodies, for example, binding to FcγRs. We generated two glycosylation variants of the same anti-PD-L1 antibody: one bearing core fucosylated N-glycans in its Fc part (92%) and its de-fucosylated counterpart (4%). The two glycosylation variants were compared to a non-glycosylated commercially available anti-PD-L1 antibody in various assays. No differences were observed regarding binding to PD-L1 and blocking of this interaction with its counter receptors PD-1 or CD80. The de-fucosylated anti-PD-L1 antibody showed increased FcγRIIIa binding resulting in enhanced antibody dependent cellular cytotoxicity (ADCC) activity against PD-L1
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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.