ArticleCancers2021
Afucosylated IgG Targets FcγRIV for Enhanced Tumor Therapy in Mice.
Article in Cancers, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Improving Anti-CTLA-4 Therapies through Peptide Masking and Fragment Crystallizable Non-fucosylation: Preclinical Characterization of Three Novel Antibodies.Clinical cancer research : an official journal of the American Association for Cancer Research · 2026Article
- Mouse Fc-FcγRIV structure guides Fc engineering for cross-species FcγR recognition.bioRxiv : the preprint server for biology · 2026Article
- A novel TM4SF4-targeting therapeutic antibody candidate with antitumor activity by blocking IGF1R and CD44 signaling and downregulating PD-L1 and B7-H4.Theranostics · 2026Article
- Enhancing the structural stability of P29-targeted monoclonal antibodies via β-hydroxybutyrylation modification improves their therapeutic performance in alveolar echinococcosis.Frontiers in cellular and infection microbiology · 2025Article
- Splenic macrophages escalate dengue disease.Nature microbiology · 2023Article
- Enhancing the therapeutic activity of hyperimmune IgG against chikungunya virus using FcγRIIIa affinity chromatography.Frontiers in immunology · 2023Article
- A novel mouse model of cutaneous T-cell lymphoma revealed the combined effect of mogamulizumab with psoralen and ultraviolet a therapy.Experimental dermatology · 2022Article
- Afucosylated IgG responses in humans - structural clues to the regulation of humoral immunity.Trends in immunology · 2022Review
- Influence of Fc Modifications and IgG Subclass on Biodistribution of Humanized Antibodies Targeting L1CAM.Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2022Article
- Role ofFrontiers in immunology · 2022Article
- Role of Fc Core Fucosylation in the Effector Function of IgG1 Antibodies.Frontiers in immunology · 2022Review
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Promising strategies for maximizing IgG effector functions rely on the introduction of natural and non-immunogenic modifications. The Fc domain of IgG antibodies contains an N-linked oligosaccharide at position 297. Human IgG antibodies lacking the core fucose in this glycan have enhanced binding to human (FcγR) IIIa/b, resulting in enhanced antibody dependent cell cytotoxicity and phagocytosis through these receptors. However, it is not yet clear if glycan-enhancing modifications of human IgG translate into more effective treatment in mouse models. We generated humanized hIgG1-TA99 antibodies with and without core-fucose. C57Bl/6 mice that were injected intraperitoneally with B16F10-gp75 mouse melanoma developed significantly less metastasis outgrowth after treatment with afucosylated hIgG1-TA99 compared to mice treated with wildtype hhIgG1-TA99. Afucosylated human IgG1 showed stronger interaction with the murine FcγRIV, the mouse orthologue of human FcγRIIIa, indicating that this glycan change is functionally conserved between the species. In agreement with this, no significant differences were observed in tumor outgrowth in FcγRIV
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