Abstract

Coronavirus disease 2019 (COVID-19) remains a major health challenge globally. Previous studies have suggested that changes in the glycosylation of IgG are closely associated with the severity of COVID-19. This study aimed to compare the profiles of IgG N-glycome between COVID-19 patients and healthy controls. A case-control study was conducted, in which 104 COVID-19 patients and 104 age- and sex-matched healthy individuals were recruited. Serum IgG N-glycome composition was analyzed by hydrophilic interaction liquid chromatography with the ultra-high-performance liquid chromatography (HILIC-UPLC) approach. COVID-19 patients have a decreased level of IgG fucosylation, which upregulates antibody-dependent cell cytotoxicity (ADCC) in acute immune responses. In severe cases, a low level of IgG sialylation contributes to the ADCC-regulated enhancement of inflammatory cytokines. The decreases in sialylation and galactosylation play a role in COVID-19 pathogenesis via the activation of the lectin-initiated alternative complement pathway. IgG N-glycosylation underlines the complex clinical phenotypes of SARS-CoV-2 infection.

Highlights

  • Coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), remains a global health challenge

  • These glycans modulate the inflammatory properties of immunoglobulin G (IgG) by changing the affinity for specific receptors and lectins [10], which are involved in the development of inflammatory diseases [11,12,13,14,15,16]

  • Progression of dengue virus (DENV) infection attributed to antibody-dependent enhancement (ADE) is proved to be regulated by specific IgG glycosylation [17]

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Summary

Introduction

Coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), remains a global health challenge. A study showed that IgG against SARS-CoV-2 S protein is characterized by afucosylation, whereas IgG against N protein has a higher level of fucosylation [20]. These findings support the notion that changes in IgG glycome composition are closely related to the loss of the immunosuppressive function and contribute to the immune-mediated pathologies of SARS-CoV-2 infection [18]. We aimed to profile the IgG N-glycome in COVID-19 patients by an age- and sex-matched case-control study

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