Science and Research

Glycosylation signature of plasma IgA of critically ill COVID-19 patients

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.

  • Potaczek, D. P.
  • van Tol, B. D. M.
  • Falck, D.
  • Krolczik, C.
  • Zlatina, K.
  • Bertrams, W.
  • Wilhelm, J.
  • Schmeck, B.
  • Seeliger, B.
  • David, S.
  • Skevaki, C.
  • Mack, E.
  • Seeger, W.
  • Schaefer, L.
  • Galuska, S. P.
  • Wuhrer, M.
  • Wygrecka, M.

Keywords

  • Humans
  • *COVID-19/immunology/blood
  • Glycosylation
  • *Immunoglobulin A/blood/immunology
  • *Critical Illness
  • *SARS-CoV-2/immunology
  • Middle Aged
  • Male
  • Female
  • *Polysaccharides/immunology/blood
  • Aged
  • Adult
  • Influenza, Human/immunology/blood
  • Respiratory Distress Syndrome/immunology/blood
  • Ards
  • Covid-19
  • NETosis
  • immunoglobulin A
Publication details
DOI: 10.3389/fimmu.2024.1439248
Journal: Front Immunol
Pages: 1439248 
Work Type: Original
Location: BREATH, UGMLC
Disease Area: PALI
Partner / Member: JLU, MHH, UMR
Access-Number: 39512344

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