2023, Volume 26, Issue 7
Engineering >> 2023, Volume 26, Issue 7 doi: 10.1016/j.eng.2022.08.007
Differences in Immunoglobulin G Glycosylation Between Influenza and COVID-19 Patients
a University Hospital Centre Zagreb, Zagreb 10000, Croatia
b Genos Glycoscience Research Laboratory, Zagreb 10000, Croatia
c Department of Cardiology, University Hospital Dubrava, Zagreb 10000, Croatia
d Faculty of Dental Medicine and Health, Josip Juraj Strossmayer University, Osijek 31000, Croatia
e Department of Biotechnology, University of Rijeka, Rijeka 51000, Croatia
f Department for Laboratory Diagnostics, University Hospital Dubrava, Zagreb 10000, Croatia
g Department for Acute Respiratory Infections, University Hospital for Infectious Diseases “Dr. Fran Mihaljević”, Zagreb 10000, Croatia
h Department for Urogenital Infections, University Hospital for Infectious Diseases “Dr. Fran Mihaljević”, Zagreb 10000, Croatia
i Department for Infectious Diseases, School of Medicine, Catholic University of Croatia, 10000 Zagreb, Croatia
j Postdoctoral Study, Faculty of Medicine, University of Rijeka, Rijeka 51000, Croatia
k Department of Maxillofacial Surgery, University of Zagreb School of Medicine, Dubrava University Hospital, Zagreb 10000, Croatia
l Faculty of Pharmacy and Biochemistry, University of Zagreb, Zagreb 10000, Croatia
m Department of Infectious Diseases, University of Zagreb School of Medicine, Zagreb 10000, Croatia
# These authors contributed equally to this work.
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Abstract
The essential role of immunoglobulin G (IgG) in immune system regulation and combatting infectious diseases cannot be fully recognized without an understanding of the changes in its N-glycans attached to the asparagine 297 of the Fc domain that occur under such circumstances. These glycans impact the antibody stability, half-life, secretion, immunogenicity, and effector functions. Therefore, in this study, we analyzed and compared the total IgG glycome—at the level of individual glycan structures and derived glycosylation traits (sialylation, galactosylation, fucosylation, and bisecting N-acetylglucosamine (GlcNAc))—of 64 patients with influenza, 77 patients with coronavirus disease 2019 (COVID-19), and 56 healthy controls. Our study revealed a significant decrease in IgG galactosylation, sialylation, and bisecting GlcNAc (where the latter shows the most significant decrease) in deceased COVID-19 patients, whereas IgG fucosylation was increased. On the other hand, IgG galactosylation remained stable in influenza patients and COVID-19 survivors. IgG glycosylation in influenza patients was more time-dependent: In the first seven days of the disease, sialylation increased and fucosylation and bisecting GlcNAc decreased; in the next 21 days, sialylation decreased and fucosylation increased (while bisecting GlcNAc remained stable). The similarity of IgG glycosylation changes in COVID-19 survivors and influenza patients may be the consequence of an adequate immune response to enveloped viruses, while the observed changes in deceased COVID-19 patients may indicate its deviation.
Keywords
Influenza ; COVID-19 ; Viral infection ; Glycosylation ; Immunoglobulin G ; Pneumonia
SupplementaryMaterials
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