ArticleRapid communications in mass spectrometry : RCM2025
Discovery and Characterization of Unusual O-Linked Glycosylation of IgG4 Antibody Using LC-MS.
Article in Rapid communications in mass spectrometry : RCM, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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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
6 citing papers in PubMed.
- Hinge-region Cys-to-Ser mutation enables homogeneous DAR6 anti-c-Met biparatopic ADCs with tolerable O-glycosylation.Antibody therapeutics · 2026Article
- Qualification and Implementation of a Robust Multi-Attribute Method Platform Across Multiple Laboratories for High-Resolution Process Characterization of Biopharmaceutical Products.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Parallel Sequencing of the Two Arms on a Bispecific Antibody by Electron Capture Dissociation on a timsOmni Platform Reveals Several By-products in the Controlled Fab-arm Exchange Process.Analytical chemistry · 2026Article
- Specific Recognition of Glycoproteins: Design Strategies and Application Prospects of Molecularly Imprinted Polymers.International journal of molecular sciences · 2026Review
- Case Report: NovelFrontiers in immunology · 2026Article
- Exploring dupilumab for asthma: from mechanistic insights to clinical outcomes, safety, and cost-effectiveness.Frontiers in pharmacology · 2025Review
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Authors and funding
3 authors.
Funding
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Abstract
backgroundConsensus is that immunoglobulin IgG4 contains only N-linked glycosylation. The analysis of several batches of commercial biopharmaceutical product Dupixent using top-down intact mass spectrometry revealed that this IgG4 features a small amount of O-linked glycosylation in the Fab region. This is the first report of an O-linked glycosylation in an IgG4 antibody.
methodsMonoclonal antibody solutions were subjected to cation exchange (CEX) and reverse phase (RP) chromatography and/or additional preconcentration/fractionation methods to prepare samples for subsequent analysis. Advanced MS analysis and fragmentation techniques (HCD, ETD, and EThcD) were employed to localize the O-linked glycosylation as well as elucidate the structure of the glycan(s).
resultsO-linked glycosylation in the IgG4 dupilumab was discovered by intact-MS. The probable location was narrowed down to four sites in the CH1 domain, and the structure of the O-linked glycan was determined to be of Core 1 type. The relative quantities of the modifications were low, but the glycosylation was consistently detected in several batches of Dupixent.
conclusionsWe discovered a rare glycosylation modification on dupilumab, an IgG4 antibody. The O-linked glycosylation was characterized and localized in the Fab region.
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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.