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Fc glycoengineering of a PD-L1 antibody harnesses Fcγ receptors for increased antitumor efficacy
Abstract
FDA-approved anti–PD-L1 monoclonal antibodies (mAbs) bear the IgG1 isotype, whose scaffolds are either wild-type (e.g., avelumab) or Fc-mutated and lacking Fcγ receptor (FcγR) engagement (e.g., atezolizumab). It is unknown whether variation in the ability of the IgG1 Fc region to engage FcγRs renders mAbs with superior therapeutic activity. In this study, we used humanized FcγR mice to study the contribution of FcγR signaling to the antitumor activity of human anti–PD-L1 mAbs and to identify an optimal human IgG scaffold for PD-L1 mAbs. We observed similar antitumor efficacy and comparable tumor immune responses in mice treated with anti–PD-L1 mAbs with wild-type and Fc-mutated IgG scaffolds. However, in vivo antitumor activity of the wild-type anti–PD-L1 mAb avelumab was enhanced by combination treatment with an FcγRIIB-blocking antibody, which was co-administered to overcome the suppressor function of FcγRIIB in the tumor microenvironment (TME). We performed Fc glycoengineering to remove the fucose subunit from the Fc-attached glycan of avelumab to enhance its binding to the activating FcγRIIIA. Treatment with the Fc-afucosylated version of avelumab also enhanced antitumor activity and induced stronger antitumor immune responses compared with the parental IgG. The enhanced effect by afucosylated PD-L1 antibody was dependent on neutrophils and associated with decreased frequencies of PD-L1 + myeloid cells and increased infiltration of T cells in the TME. Our data reveal that the current design of FDA-approved anti–PD-L1 mAbs does not optimally harness FcγR pathways and suggest two strategies to enhance FcγR engagement to optimize anti–PD-L1 immunotherapy.
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Immune checkpoint inhibitors as monotherapy have limited efficacy in the treatment of relapsed/refractory multiple myeloma.
“However, the efficacy of these antibodies particularly as monotherapy was limited in the treatment of RRMM [173–176].”
From Multiple myeloma: signaling pathways and targeted therapy (2024) · cites this paper as [176]
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Metadata
- Authors
- Cohen Saban, N., Yalin, A., Landsberger, T., Salomon, R., Alva, A., Feferman, T., Amit, I., & Dahan, R.
- Affiliations
- Department of Systems Immunology, Weizmann Institute of Science, Rehovot, Israel.
- Weizmann Institute of Science (IL)
- U-M Rogel Cancer Center (US)
- Corresponding author
- Dahan, Rony
- ORCID
- Venue
- Science Immunology
- Published
- 2023-03-31
- Volume
- 8
- Issue
- 81
- Pages
- eadd8005-eadd8005
- ISSN
- 2470-9468 (ISSN-L)
- OpenAlex
- W4323031408
- Cited by
- 39
- References
- 55
- Citations by year
- 2026: 6 · 2025: 9 · 2024: 16 · 2023: 8
- FWCI
- 6.43
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science Immunology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Health Sciences › Medicine › Oncology › Cancer Immunotherapy and Biomarkers
- Life Sciences › Immunology and Microbiology › Immunology › Immune Cell Function and Interaction
- Keywords
- anti-PD-L1 monoclonal antibody, Fc gamma receptor, FcγRIIB, FcγRIIIa, avelumab, tumor microenvironment, neutrophils, myeloid cells, T cell infiltration, cancer immunotherapy
- MeSH terms
- Immune Checkpoint Inhibitors, Animals, Antibodies, Monoclonal, Humans, Immunoglobulin G, Immunotherapy, Receptors, IgG, Mice
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