ArticlePloS one2012
Analysis and functional consequences of increased Fab-sialylation of intravenous immunoglobulin (IVIG) after lectin fractionation.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers, 1 of them a synthesis that pooled it.
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Who cites it
51 citing papers in PubMed, 1 synthesis or guideline pooled it, 121 citations in OpenAlex.
- Efficacy and safety of blood derivatives therapy in Alzheimer's disease: a systematic review and meta-analysis.Systematic reviews · 2022Pooled it
- Trial
- Intravenous immunoglobulin remodels innate immune cell communication and induces differential autophagy pathways in Kawasaki disease.Frontiers in immunology · 2026Article
- Computational analysis reveals non-consensus N-glycosylation sequons in antibody Fab region.mAbs · 2025Article
- Modulation of immunoglobulin G oligomerization by variable domain glycans: A mechanism to regulate complement activation.PNAS nexus · 2025Article
- Elevated Fab glycosylation of autoantibodies maintained during B cell depletion therapy.Scientific reports · 2025Article
- Immunoglobulins: Mechanistic Approaches in Moderation of Various Inflammatory and Anti-inflammatory Pathways.Current pharmaceutical biotechnology · 2025Review
- The role of antibody glycosylation in autoimmune and alloimmune kidney diseases.Nature reviews. Nephrology · 2024Review
- Unveiling the multifaceted landscape of N-glycosylation in antibody variable domains: Insights and implications.International journal of biological macromolecules · 2024Article
- Decipher the Immunopathological Mechanisms and Set Up Potential Therapeutic Strategies for Patients with Lupus Nephritis.International journal of molecular sciences · 2023Review
- Mechanism underlying polyvalent IgG-induced regulatory T cell activation and its clinical application: Anti-idiotypic regulatory T cell theory for immune tolerance.Frontiers in immunology · 2023Review
- IgG Anti-Citrullinated Protein Antibody Variable Domain Glycosylation Increases Before the Onset of Rheumatoid Arthritis and Stabilizes Thereafter: A Cross-Sectional Study Encompassing ~1,500 Samples.Arthritis & rheumatology (Hoboken, N.J.) · 2022Article
- Strategies to control therapeutic antibody glycosylation during bioprocessing: Synthesis and separation.Biotechnology and bioengineering · 2022Review
- Sialylated immunoglobulin G: a promising diagnostic and therapeutic strategy for autoimmune diseases.Theranostics · 2021Review
- Sialylated Immunoglobulins for the Treatment of Immuno-Inflammatory Diseases.International journal of molecular sciences · 2020Review
- High-Dose Intravenous Immunoglobulins in the Treatment of Severe Acute Viral Pneumonia: The Known Mechanisms and Clinical Effects.Frontiers in immunology · 2020Review
- Engineering of Fc Multimers as a Protein Therapy for Autoimmune Disease.Frontiers in immunology · 2020Review
- A Comparison of Immunoglobulin Variable Region N-Linked Glycosylation in Healthy Donors, Autoimmune Disease and Lymphoma.Frontiers in immunology · 2020Review
- Lectin-Based Method for Deciphering Human Milk IgG Sialylation.Molecules (Basel, Switzerland) · 2019Article
- Human DC-SIGN and CD23 do not interact with human IgG.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has been proposed that the anti-inflammatory effects of intravenous immunoglobulin (IVIG) might be due to the small fraction of Fc-sialylated IgG. In this study we biochemically and functionally characterized sialic acid-enriched IgG obtained by Sambucus nigra agglutinin (SNA) lectin fractionation. Two main IgG fractions isolated by elution with lactose (E1) or acidified lactose (E2) were analyzed for total IgG, F(ab')(2) and Fc-specific sialic acid content, their pattern of specific antibodies and anti-inflammatory potential in a human in vitro inflammation system based on LPS- or PHA-stimulated whole blood. HPLC and LC-MS testing revealed an increase of sialylated IgG in E1 and more substantially in the E2 fraction. Significantly, the increased amount of sialic acid residues was primarily found in the Fab region whereas only a minor increase was observed in the Fc region. This indicates preferential binding of the Fab sialic acid to SNA. ELISA analyses of a representative range of pathogen and auto-antigens indicated a skewed antibody pattern of the sialylated IVIG fractions. Finally, the E2 fraction exerted a more profound anti-inflammatory effect compared to E1 or IVIG, evidenced by reduced CD54 expression on monocytes and reduced secretion of MCP-1 (CCL2); again these effects were Fab- but not Fc-dependent. Our results show that SNA fractionation of IVIG yields a minor fraction (approx. 10%) of highly sialylated IgG, wherein the sialic acid is mainly found in the Fab region. The tested anti-inflammatory activity was associated with Fab not Fc sialylation.
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