tetano
Editor, Senior Moderator
Front Immunol
. 2024 Oct 24:15:1439248.
doi: 10.3389/fimmu.2024.1439248. eCollection 2024. Glycosylation signature of plasma IgA of critically ill COVID-19 patients
Daniel P Potaczek[SUP] 1 2 3 [/SUP], Bianca D M van Tol[SUP] 4 [/SUP], David Falck[SUP] 4 [/SUP], Christina Krolczik[SUP] 1 [/SUP], Kristina Zlatina[SUP] 5 [/SUP], Wilhelm Bertrams[SUP] 6 [/SUP], Jochen Wilhelm[SUP] 7 [/SUP], Bernd Schmeck[SUP] 6 [/SUP], Benjamin Seeliger[SUP] 8 9 [/SUP], Sascha David[SUP] 10 [/SUP], Chrysanthi Skevaki[SUP] 11 [/SUP], Elisabeth Mack[SUP] 12 [/SUP], Werner Seeger[SUP] 7 13 [/SUP], Liliana Schaefer[SUP] 14 [/SUP], Sebastian P Galuska[SUP] 5 [/SUP], Manfred Wuhrer[SUP] 4 [/SUP], Małgorzata Wygrecka[SUP] 1 7 13 [/SUP]
Affiliations
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.
Keywords: ARDS; COVID-19; NETosis; glycosylation; immunoglobulin A.
. 2024 Oct 24:15:1439248.
doi: 10.3389/fimmu.2024.1439248. eCollection 2024. Glycosylation signature of plasma IgA of critically ill COVID-19 patients
Daniel P Potaczek[SUP] 1 2 3 [/SUP], Bianca D M van Tol[SUP] 4 [/SUP], David Falck[SUP] 4 [/SUP], Christina Krolczik[SUP] 1 [/SUP], Kristina Zlatina[SUP] 5 [/SUP], Wilhelm Bertrams[SUP] 6 [/SUP], Jochen Wilhelm[SUP] 7 [/SUP], Bernd Schmeck[SUP] 6 [/SUP], Benjamin Seeliger[SUP] 8 9 [/SUP], Sascha David[SUP] 10 [/SUP], Chrysanthi Skevaki[SUP] 11 [/SUP], Elisabeth Mack[SUP] 12 [/SUP], Werner Seeger[SUP] 7 13 [/SUP], Liliana Schaefer[SUP] 14 [/SUP], Sebastian P Galuska[SUP] 5 [/SUP], Manfred Wuhrer[SUP] 4 [/SUP], Małgorzata Wygrecka[SUP] 1 7 13 [/SUP]
Affiliations
- PMID: 39512344
- PMCID: PMC11541231
- DOI: 10.3389/fimmu.2024.1439248
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.
Keywords: ARDS; COVID-19; NETosis; glycosylation; immunoglobulin A.