ArticleFrontiers in immunology2022
Site-specific N-glycosylation characterization of micro monoclonal immunoglobulins based on EThcD-sceHCD-MS/MS.
Article in Frontiers in immunology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 16 citations in OpenAlex.
- The N‑Glycoproteomic Landscape of the Lung in Monocrotaline-Induced Pulmonary Arterial Hypertension.ACS omega · 2026Article
- Semantic annotation of Glycomics and Glycoproteomics methods.Glycobiology · 2026Article
- Quantitative N-glycoproteomic analysis reveals glycosylation signatures of plasma immunoglobulin G in systemic sclerosis.Frontiers in immunology · 2025Article
- GlycoIP: an integrated platform for simultaneous and site-specificFrontiers in chemistry · 2025Article
- N-glycosylation patterns of plasma immunoglobulin G in anti-synthetase syndrome disease.Frontiers in immunology · 2025Article
- Quantitative site-specific N-glycosylation analysis reveals IgG glyco-signatures for pancreatic cancer diagnosis.Clinical proteomics · 2024Article
- Developing glycoproteomics reveals the role of posttranslational glycosylation in the physiological and pathological processes of male reproduction.iMetaOmics · 2024Article
- Site-Specific Quantitative N-Glycoproteomics: The Great Clinical Application Potential of GlycoQuant.Phenomics (Cham, Switzerland) · 2024Article
- A Novel Integrated Pipeline for Site-Specific Quantification of N-glycosylation.Phenomics (Cham, Switzerland) · 2024Article
- Editorial: New methods, techniques and applications in clinical glycoproteomics.Frontiers in molecular biosciences · 2023Article
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Authors and funding
8 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Monoclonal immunoglobulin produced by clonal plasma cells is the main cause in multiple myeloma and monoclonal gammopathy of renal significance. Because of the complicated purification method and the low stoichiometry of purified protein and glycans, site-specific N-glycosylation characterization for monoclonal immunoglobulin is still challenging. To profile the site-specific N-glycosylation of monoclonal immunoglobulins is of great interest. Therefore, in this study, we presented an integrated workflow for micro monoclonal IgA and IgG purification from patients with multiple myeloma in the HYDRASYS system, in-agarose-gel digestion, LC-MS/MS analysis without intact N-glycopeptide enrichment, and compared the identification performance of different mass spectrometry dissociation methods (EThcD-sceHCD, sceHCD, EThcD and sceHCD-pd-ETD). The results showed that EThcD-sceHCD was a better choice for site-specific N-glycosylation characterization of micro in-agarose-gel immunoglobulins (~2 μg) because it can cover more unique intact N-glycopeptides (37 and 50 intact N-glycopeptides from IgA1 and IgG2, respectively) and provide more high-quality spectra than sceHCD, EThcD and sceHCD-pd-ETD. We demonstrated the benefits of the alternative strategy in site-specific N-glycosylation characterizing micro monoclonal immunoglobulins obtained from bands separated by electrophoresis. This work could promote the development of clinical N-glycoproteomics and related immunology.
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