Frontiers in immunology · 2022
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, Trapé Átila Alexandre, Fendel Rolf, de Miranda Santos Isabel Kinney Ferreira, Wuhrer Manfred, ImmunoCovid Consortium
Аннотация
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.