The IgG glycome of SARS-CoV-2 infected individuals reflects disease course and severity.
Front Immunol
; 13: 993354, 2022.
Article
de En
| MEDLINE
| ID: mdl-36389824
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.
Mots clés
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Immunoglobuline G
/
COVID-19
Type d'étude:
Prognostic_studies
Limites:
Humans
Langue:
En
Journal:
Front Immunol
Année:
2022
Type de document:
Article
Pays d'affiliation:
Pays-Bas