ArticleBiochemistry2012
NMR characterization of immunoglobulin G Fc glycan motion on enzymatic sialylation.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed, 118 citations in OpenAlex.
- Fast NMR-Based Assessment of Cancer-Associated Protein Glycosylations from Serum Samples.Analytical chemistry · 2025Article
- Unique Glycans in Synaptic Glycoproteins in Mouse Brain.ACS chemical neuroscience · 2024Article
- The role of antibody glycosylation in autoimmune and alloimmune kidney diseases.Nature reviews. Nephrology · 2024Review
- A comprehensive assessment of selective amino acidJournal of biomolecular NMR · 2024Article
- Primary Structure of Glycans by NMR Spectroscopy.Chemical reviews · 2023Review
- Mass Spectrometry-Based Methods to Determine the Substrate Specificities and Kinetics of N-Linked Glycan Hydrolysis by Endo-β-N-Acetylglucosaminidases.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Extensive substrate recognition by the streptococcal antibody-degrading enzymes IdeS and EndoS.Nature communications · 2022Article
- Quantifying Carbohydrate-Active Enzyme Activity with Glycoprotein Substrates Using Electrospray Ionization Mass Spectrometry and Center-of-Mass Monitoring.Analytical chemistry · 2021Article
- Importance and Monitoring of Therapeutic Immunoglobulin G Glycosylation.Experientia supplementum (2012) · 2021Review
- Characterizing human α-1,6-fucosyltransferase (FUT8) substrate specificity and structural similarities with related fucosyltransferases.The Journal of biological chemistry · 2020Article
- Impact of IgG1 N-glycosylation on their interaction with Fc gamma receptors.Current research in immunology · 2020Article
- Enhancement of sialylation in rIgG in glyco-engineered Chinese hamster ovary cells.Cytotechnology · 2020Article
- Antigen-Induced Allosteric Changes in a Human IgG1 Fc Increase Low-Affinity Fcγ Receptor Binding.Structure (London, England : 1993) · 2020Article
- A synopsis of recent developments defining how N-glycosylation impacts immunoglobulin G structure and function.Glycobiology · 2020Review
- Considerations of Antibody Geometric Constraints on NK Cell Antibody Dependent Cellular Cytotoxicity.Frontiers in immunology · 2020Review
- The Impact of Immunoglobulin G1 Fc Sialylation on Backbone Amide H/D Exchange.Antibodies (Basel, Switzerland) · 2019Article
- Glycoprofile Analysis of an Intact Glycoprotein As Inferred by NMR Spectroscopy.ACS central science · 2019Article
- Article
- CmAbs · 2019Article
- Macro- and Micro-Heterogeneity of Natural and Recombinant IgG Antibodies.Antibodies (Basel, Switzerland) · 2019Review
18 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The terminal carbohydrate residues of the N-glycan on the immunoglobulin G (IgG) fragment crystallizable (Fc) determine whether IgG activates pro- or anti-inflammatory receptors. The IgG Fc alone becomes potently anti-inflammatory upon addition of α2-6-linked N-acetylneuraminic acid residues to the N-glycan, stimulating interest in use of this entity in novel therapies for autoimmune disease [Kaneko et al. (2006) Science313, 670-3]. Complete Fc sialylation has, however, been deemed challenging due to a combination of branch specificity and perceived protection by glycan-protein interactions. Here we report the preparation of high levels of disialylated Fc by using sufficient amounts of a highly active α2-6 sialyltransferase (ST6Gal1) preparation expressed in a transiently transformed human cell culture. Surprisingly, ST6Gal1 sialylated the two termini of the complex-type binantennary glycan in a manner remarkably similar to that observed for the free N-glycan, suggesting the Fc polypeptide does not greatly influence ST6Gal1 specificity. In addition, sialylation of either branch terminus does not appear to dramatically alter the motional behavior of the N-glycan as judged by solution NMR spectroscopy. Together these, data suggest the N-glycan occupies two distinct states: one with both glycan termini sequestered from enzymatic modification by an α1-6Man-branch interaction with the polypeptide surface and the other with both glycan termini exposed to the bulk solvent and free from glycan-polypeptide interactions. The results suggest new modes by which disialylated Fc can act as an anti-inflammatory effector.
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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.