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Published on: July 13, 2017
Profile of Immunoglobulin G N-Glycome in COVID-19 Patients: A Case-Control Study
Haifeng Hou1, Huan Yang2,3, Pengcheng Liu1
1School of Public Health, Shandong First Medical University & Shandong Academy of Medical Sciences, Tai'an, China.
Insights
Changes in IgG glycosylation impact COVID-19 severity. This study found decreased IgG fucosylation and sialylation in patients, affecting immune responses and disease pathogenesis.
Area of Science:
- Immunology
- Glycobiology
- Infectious Diseases
Background:
- Coronavirus disease 2019 (COVID-19) poses a global health challenge.
- Alterations in immunoglobulin G (IgG) glycosylation patterns are linked to COVID-19 severity.
Purpose of the Study:
- To compare IgG N-glycome profiles between COVID-19 patients and healthy controls.
- To investigate the association between IgG glycosylation changes and COVID-19 pathogenesis.
Main Methods:
- A case-control study involving 104 COVID-19 patients and 104 healthy controls.
- Serum IgG N-glycome composition analyzed using hydrophilic interaction liquid chromatography with ultra-high-performance liquid chromatography (HILIC-UPLC).
Main Results:
- COVID-19 patients exhibited decreased IgG fucosylation, potentially upregulating antibody-dependent cell cytotoxicity (ADCC).
- Severe COVID-19 cases showed reduced IgG sialylation, contributing to ADCC-enhanced inflammatory cytokines.
- Decreased IgG sialylation and galactosylation were implicated in COVID-19 pathogenesis via complement pathway activation.
Conclusions:
- IgG N-glycosylation patterns are significantly altered in COVID-19 patients.
- These glycosylation changes are associated with altered immune responses, including ADCC and complement activation.
- IgG N-glycosylation plays a crucial role in the complex clinical manifestations of SARS-CoV-2 infection.
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.
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