The IgG glycome of SARS-CoV-2 infected individuals reflects disease course and severity

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Siekman, Sterre L. ; Pongracz, Tamas ; Wang, Wenjun ; Nouta, Jan ; Kremsner, Peter G. ; da Silva-Neto, Pedro Vieira ; Esen, Meral ; Kreidenweiss, Andrea ; Held, Jana ; Trape, Atila Alexandre ; Fendel, Rolf ; de Miranda Santos, Isabel Kinney Ferreira ; Wuhrer, Manfred

• Document type: Journal article
• Source: FRONTIERS IN IMMUNOLOGY; v. 13, p. 13-pg., 2022-10-18.

Abstract

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. (AU)

• FAPESP's process: 20/05207-6 - Prospective evaluation of lipid mediators production on the immune response against COVID-19: search for biomarkers and new therapeutic targets in the evolution of the disease
• Grantee: Lúcia Helena Faccioli
• Support Opportunities: Regular Research Grants