Monoclonal antibody N-glycosylation profiling using capillary electrophoresis – Mass spectrometry: Assessment and method validation
Open accessAbstract
Characterization of therapeutic proteins represents a major challenge for analytical sciences due to their heterogeneity caused by post-translational modifications (PTM). Among these PTM, glycosylation which is possibly the most prominent, require comprehensive identification because of their major influence on protein structure and effector functions of monoclonal antibodies (mAbs). As a consequence, glycosylation profiling must be deeply characterized. For this application, several analytical methods such as separation-based or MS-based methods, were evaluated. However, no CE-ESI-MS approach has been assessed and validated. Here, we illustrate how the use of CE-ESI-MS method permits the comprehensive characterization of mAbs N-glycosylation at the glycopeptide level to perform relative quantitation of N-glycan species. Validation of the CE-ESI-MS method in terms of robustness and reproducibility was demonstrated through the relative quantitation of glycosylation profiles for ten different mAbs produced in different cell lines. Glycosylation patterns obtained for each mAbs were compared to Hydrophilic Interaction Chromatography of 2-aminobenzamide labelled glycans with fluorescence detector (HILIC-FD) analysis considered as a reference method. Very similar glycoprofiling were obtained with the CE-ESI-MS and HILIC-FD demonstrating the attractiveness of CE-ESI-MS method to characterize and quantify the glycosylation heterogeneity of a wide range of therapeutic mAbs with high accuracy and precision.
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CZE separation has frequently been used to analyze glycosylated peptides and glycans, and CZE via TDMS has been used for glycosylation characterization.
“CZE separation has frequently been used to analyze glycosylated peptides and glycans49,57,80,81 and CZE separation via TDMS was used for glycosylation characterization82.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [80]
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- Authors
- Giorgetti, J., D’Atri, V., Canonge, J., Lechner, A., Guillarme, D., Colas, O., Wagner-Rousset, E., Beck, A., Leize-Wagner, E., & François, Y.-N.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- University of Geneva (CH)
- Center of Immunology Pierre Fabre (FR)
- Corresponding author
- François, Yannis-Nicolas
- ORCID
- Venue
- Talanta
- Publisher
- Elsevier BV
- Published
- 2018-02
- Volume
- 178
- Pages
- 530-537
- ISSN
- 0039-9140 (ISSN-L)
- OpenAlex
- W2763901610
- Cited by
- 65
- References
- 30
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 4 · 2023: 2 · 2022: 11 · 2021: 8 · 2020: 12 · 2019: 14 · 2018: 6
- FWCI
- 3.58
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Talanta (acceptedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (publishedVersion, other-oa)
- HAL (submittedVersion, other-oa)
- HAL (submittedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- univOAK (4 institutions : Université de Strasbourg, Université de Haute Alsace, INSA Strasbourg, Bibliothèque Nationale et Universitaire de Strasbourg) (submittedVersion, cc-by-nc)
- Funders
- Centre National de la Recherche Scientifique (UMR 7140)
- Université de Strasbourg
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (31003A_159494)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Immunology and Microbiology › Immunology › Biosimilars and Bioanalytical Methods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- monoclonal antibodies, N-glycosylation, glycopeptide profiling, capillary electrophoresis, electrospray ionization mass spectrometry, method validation, therapeutic proteins, post-translational modification, glycosylation heterogeneity
- MeSH terms
- Antibodies, Monoclonal, Chromatography, Glycopeptides, Glycosylation, Reproducibility of Results, Electrophoresis, Capillary, Spectrometry, Mass, Electrospray Ionization
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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