The IgG glycome of SARS-CoV-2 infected individuals reflects disease course and severity
- Resource Type
- Authors
- Sterre L, Siekman; Tamas, Pongracz; Wenjun, Wang; Jan, Nouta; Peter G, Kremsner; Pedro Vieira, da Silva-Neto; Meral, Esen; Andrea, Kreidenweiss; Jana, Held; Átila Alexandre, Trapé; Rolf, Fendel; Isabel Kinney Ferreira, de Miranda Santos; Manfred, Wuhrer; Kamila, Zaparoli
- Source
- Frontiers in Immunology, 13. FRONTIERS MEDIA SA
- Subject
- Glycosylation
SARS-CoV-2
Immunoglobulin G
IgG glycosylation
Immunology
total IgG
Humans
Immunology and Allergy
COVID-19
Biomarkers
anti-spike IgG
- Language
- English
Immunoglobulin G (IgG) antibodies play an important role in the immune response against viruses such as SARS-CoV-2. As the effector functions of IgG are modulated by N-glycosylation of the Fc region, the structure and possible function of the IgG N-glycome has been under investigation in relation to divergent COVID-19 disease courses. Through LC-MS analysis we studied both total IgG1 and spike protein-specific IgG1 Fc glycosylation of 129 German and 163 Brazilian COVID-19 patients representing diverse patient populations. We found that hospitalized COVID-19 patients displayed decreased levels of total IgG1 bisection and galactosylation and lowered anti-S IgG1 fucosylation and bisection as compared to mild outpatients. Anti-S IgG1 glycosylation was dynamic over the disease course and both anti-S and total IgG1 glycosylation were correlated to inflammatory markers. Further research is needed to dissect the possible role of altered IgG glycosylation profiles in (dys)regulating the immune response in COVID-19.