ArticleGlycobiology2017
Glycosylation of MUC1 influences the binding of a therapeutic antibody by altering the conformational equilibrium of the antigen.
Article in Glycobiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 70 citations in OpenAlex.
- Structural Basis of a High-Affinity Antibody Binding to Glycoprotein with Glycocalyx Decay.JACS Au · 2026Article
- From Glycocode to Precision Oncology: Therapeutic Strategies Targeting Aberrant O-GalNAc Glycosylation in Cancer.Chemical reviews · 2026Review
- Engineering programmable CAR and antigen pairing via drug-gated light activation.Nature communications · 2026Article
- Structure-guided phage display discovery of antibodies for (S)Tn-glycans in protein context.Nature chemical biology · 2026Article
- Mucin expression in pancreatic ductal adenocarcinoma cell lines in 2D and 3D cultures: A proteomic and immunocytochemical analysis.PloS one · 2026Article
- Article
- Development of uMUC-1 Targeted NEMO Particles with pH-Activatable MRI Signals for Enhanced Detection of Malignant Breast Cancer Cells.ACS applied bio materials · 2025Article
- Structure of the Fab fragment of a humanized 5E5 antibody to a cancer-specific Tn-MUC1 epitope.Acta crystallographica. Section D, Structural biology · 2025Article
- Single cell RNA-seq and bulk RNA-seq analysis identifies MUC1 as a key gene for lung adenocarcinoma to neuroendocrine transformation.Translational lung cancer research · 2025Article
- Subcellular Fractionation Enables Assessment of Nucleotide Sugar Donors Inside the Golgi Apparatus as a Prerequisite for Unraveling Culture Impacts on Glycoforms of Antibodies.Biotechnology journal · 2025Article
- Article
- Prognostic implications of MUC1 and XBP1 concordant expression in multiple myeloma: A retrospective study.PloS one · 2025Article
- The Glycoworld: Glycoproteins in Nature: A General Overview of the Different Roles That Glycoproteins Exert in Living Organism.Methods in molecular biology (Clifton, N.J.) · 2025Review
- Antibody-Antigen Epitope Mapping by X-Ray Crystallography.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Multi-armored allogeneic MUC1 CAR T cells enhance efficacy and safety in triple-negative breast cancer.Science advances · 2024Article
- Structural Basis for Multivalent MUC16 Recognition and Robust Anti-Pancreatic Cancer Activity of Humanized Antibody AR9.6.Molecular cancer therapeutics · 2024Article
- Reverse-engineering the anti-MUC1 antibody 139H2 by mass spectrometry-based de novo sequencing.Life science alliance · 2024Article
- Structure-Guided Approach for the Development of MUC1-Glycopeptide-Based Cancer Vaccines with Predictable Responses.JACS Au · 2024Article
- Targeting Solid Cancers with a Cancer-Specific Monoclonal Antibody to Surface Expressed Aberrantly O-glycosylated Proteins.Molecular cancer therapeutics · 2023Article
- Review
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
In cancer cells, the glycoprotein Mucin 1 (MUC1) undergoes abnormal, truncated glycosylation. The truncated glycosylation exposes cryptic peptide epitopes that can be recognized by antibodies. Since these immunogenic regions are cancer specific, they represent ideal targets for therapeutic antibodies. We investigated the role of tumor-specific glycosylation on antigen recognition by the therapeutic antibody AR20.5. We explored the affinity of AR20.5 to a synthetic cancer-specific MUC1 glycopeptide and peptide. The antibody bound to the glycopeptide with an order of magnitude stronger affinity than the naked peptide. Given these results, we postulated that AR20.5 must specifically bind the carbohydrate as well as the peptide. Using X-ray crystallography, we examined this hypothesis by determining the structure of AR20.5 in complex with both peptide and glycopeptide. Surprisingly, the structure revealed that the carbohydrate did not form any specific polar contacts with the antibody. The high affinity of AR20.5 for the glycopeptide and the lack of specific binding contacts support a hypothesis that glycosylation of MUC1 stabilizes an extended bioactive conformation of the peptide recognized by the antibody. Since high affinity binding of AR20.5 to the MUC1 glycopeptide may not driven by specific antibody-antigen contacts, but rather evidence suggests that glycosylation alters the conformational equilibrium of the antigen, which allows the antibody to select the correct conformation. This study suggests a novel mechanism of antibody-antigen interaction and also suggests that glycosylation of MUC1 is important for the generation of high affinity therapeutic antibodies.
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