ArticlemAbs
Engineered Fc-glycosylation switch to eliminate antibody effector function.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 14 citations in OpenAlex.
- IMGT-NC Engineered Variants of INN Therapeutic IG or Antibodies and Related IgSF Proteins (TR, FPIA and CPCA): Bridging Sequences, Structures and Functions for AI.Biomolecules · 2026Review
- Selective Depletion of Autoreactive Plasma Cells as a Novel Strategy to Treat Acetylcholine Receptor Antibody-Positive Myasthenia Gravis.European journal of immunology · 2026Article
- Turncoat antibodies unmasked in a model of autoimmune demyelination: From biology to therapy.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Precemtabart tocentecan, an anti-CEACAM5 antibody-drug conjugate, in metastatic colorectal cancer: a phase 1 trial.Nature medicine · 2025Article
- PK/PD Evaluation of Antibody-Drug Conjugates with Enhanced Immune Effector Functions.The AAPS journal · 2024Article
- Dynamics of antibody engagement of red blood cellsFrontiers in immunology · 2024Article
- Antibody-drug conjugates: the paradigm shifts in the targeted cancer therapy.Frontiers in immunology · 2023Review
- Ex silico engineering of cystine-dense peptides yielding a potent bispecific T cell engager.Science translational medicine · 2022Article
- Impact of Drug Conjugation on Thermal and Metabolic Stabilities of Aglycosylated andBioconjugate chemistry · 2022Article
- Site-Specific Antibody Conjugation to Engineered Double Cysteine Residues.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Application of an integrated computational antibody engineering platform to design SARS-CoV-2 neutralizers.Antibody therapeutics · 2021Article
- Article
Corrections and comments
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Authors and funding
14 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibodies mediate effector functions through Fcγ receptor (FcγR) interactions and complement activation, causing cytokine release, degranulation, phagocytosis, and cell death. They are often undesired for development of therapeutic antibodies where only antigen binding or neutralization would be ideal. Effector elimination has been successful with extensive mutagenesis, but these approaches can potentially lead to manufacturability and immunogenicity issues. By switching the native glycosylation site from position 297 to 298, we created alternative antibody glycosylation variants in the receptor interaction interface as a novel strategy to eliminate the effector functions. The engineered glycosylation site at Asn298 was confirmed by SDS-PAGE, mass spectrometry, and X-ray crystallography (PDB code 6X3I). The lead NNAS mutant (S298N/T299A/Y300S) shows no detectable binding to mouse or human FcγRs by surface plasmon resonance analyses. The effector functions of the mutant are completely eliminated when measured in antibody-dependent cell-meditated cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC) assays.
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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.