ArticleGlycobiology2022
ST6Gal1 in plasma is dispensable for IgG sialylation.
Article in Glycobiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- Aberrant glycosylation in hematologic malignancies: mechanisms, immune evasion, and therapeutic targeting.Blood cancer journal · 2026Review
- Immunoglobulin G N-glycosylation remodeling in viral infections: immunomodulatory roles and potential biomarker implications.Frontiers in immunology · 2026Review
- Endothelial cells sialylate IgG within the FcRn-mediated recycling pathway.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- B-Cell ST6Gal1/Neuraminidase 1 Ratios Inversely Predict the Combined Remission and Low-Disease-Activity Subgroup with DAS28-MCP-1 and SDAI Scores for Rheumatoid Arthritis.International journal of molecular sciences · 2025Article
- Deep humoral profiling coupled to interpretable machine learning unveils diagnostic markers and pathophysiology of schistosomiasis.Science translational medicine · 2024Article
- Sialic acid in the regulation of blood cell production, differentiation and turnover.Immunology · 2024Review
- IgM N-glycosylation correlates with COVID-19 severity and rate of complement deposition.Nature communications · 2024Article
- IgG sialylation occurs in B cells pre antibody secretion.Frontiers in immunology · 2024Article
- Platelet-localized ST6Gal1 does not impact IgG sialylation.Glycobiology · 2023Article
- Effect of posttranslational modifications and subclass on IgG activity: from immunity to immunotherapy.Nature immunology · 2023Review
- Control of lupus activity during pregnancy via the engagement of IgG sialylation: novel crosstalk between IgG sialylation and pDC functions.Frontiers of medicine · 2023Article
- IgG N-glycan Signatures as Potential Diagnostic and Prognostic Biomarkers.Diagnostics (Basel, Switzerland) · 2023Review
- A signature based on glycosyltransferase genes provides a promising tool for the prediction of prognosis and immunotherapy responsiveness in ovarian cancer.Journal of ovarian research · 2023Article
- The role ofFrontiers in immunology · 2023Review
- Reply to Werner and Nimmerjahn letter to the Glyco-Forum.Glycobiology · 2022Article
- Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update for 2021-2022.Mass spectrometry reviewsReview
Corrections and comments
- Commented on by
- Commented on by
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The glycosylation of immunoglobulin G (IgG) has attracted increased attention due to the impact of N-glycan modifications at N297 on IgG function, acting primarily through modulation of Fc domain conformation and Fcγ receptor-binding affinities and signaling. However, the mechanisms regulating IgG glycosylation and especially α2,6-sialylation of its N-glycan remain poorly understood. We observed previously that IgG is normally sialylated in mice with B cells lacking the sialyltransferase ST6Gal1. This supported the hypothesis that IgG may be sialylated outside of B cells, perhaps through the action of hepatocyte-released plasma ST6Gal1. Here, we demonstrate that this model is incorrect. Animals lacking hepatocyte expressed ST6Gal1 retain normal IgG α2,6-sialylation despite the lack of detectable ST6Gal1 in plasma. Moreover, we confirmed that B cells were not a redundant source of IgG sialylation. Thus, while α2,6-sialylation is lacking in IgG from mice with germline ablation of ST6Gal1, IgG α2,6-sialylation is normal in mice lacking ST6Gal1 in either hepatocytes or B cells. These results indicate that IgG α2,6-sialylation arises after release from a B cell but is not dependent on plasma-localized ST6Gal1 activity.
Indexed as
Identifiers
What OpenQuestion holds
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.