ArticleFrontiers in immunology2024
Glycosylation signature of plasma IgA of critically ill COVID-19 patients.
Article in Frontiers in immunology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Extracellular RNA clearance by non-canonical cell-surface MDA5 protects against lung fibrosis.EMBO molecular medicine · 2026Article
- Large glycomics datasets as a tool to understand the function of glycans.Nature chemical biology · 2026Review
- Research Advances and Biological Features of IgA for Immune-Related Diseases.International journal of molecular sciences · 2026Review
- Bovine Lactoferrin Modulates Mononuclear Cell Activity in Human Palatine Tonsils.International journal of molecular sciences · 2026Article
- Anti-SARS-CoV-2 nucleoprotein IgA is associated with worse disease severity in critically ill COVID-19 pneumonia patients.Frontiers in immunology · 2026Article
- Immunoglobulin G N-glycosylation remodeling in viral infections: immunomodulatory roles and potential biomarker implications.Frontiers in immunology · 2026Review
- Anti-SARS-CoV-2 Spike IgA2 Induces Inflammation by Human Macrophages.European journal of immunology · 2025Article
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Authors and funding
17 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thromboembolic complications are common in severe COVID-19 and are thought to result from excessive neutrophil-extracellular-trap (NET)-driven immunothrombosis. Glycosylation plays a vital role in the efficiency of immunoglobulin A (IgA) effector functions, with significant implications for NET formation in infectious diseases. This study represents the first comprehensive analysis of plasma IgA glycosylation during severe SARS-CoV-2 or Influenza A infection, revealing lower sialylation and higher galactosylation of IgA1 O-glycans in acute respiratory distress syndrome (ARDS), regardless of the underlying cause of the disease. Importantly, N-glycans displayed an infection-specific pattern, with N47 of IgA2 showing diminished sialylation and bisection, and N340/N327 of IgA1/2 demonstrating lower fucosylation and antennarity along with higher non-complex glycans in COVID-19 compared to Influenza. Notably, COVID-19 IgA possessed strong ability to induce NET formation and its glycosylation patterns correlated with extracellular DNA levels in plasma of critically ill COVID-19 patients. Our data underscores the necessity of further research on the role of IgA glycosylation in the modulation of pathogen-specific immune responses in COVID-19 and other infectious diseases.
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