• Medientyp: E-Artikel
  • Titel: IgM N-glycosylation correlates with COVID-19 severity and rate of complement deposition
  • Beteiligte: Haslund-Gourley, Benjamin S.; Woloszczuk, Kyra; Hou, Jintong; Connors, Jennifer; Cusimano, Gina; Bell, Mathew; Taramangalam, Bhavani; Fourati, Slim; Mege, Nathan; Bernui, Mariana; Altman, Matthew C.; Krammer, Florian; van Bakel, Harm; Ozonoff, Al; Ehrlich, Lauren I. R.; Melamed, Esther; Sesma, Ana Fernandez; Simon, Viviana; Pulendran, Bali; Nadeau, Kari C.; Davis, Mark M.; McCoey, Grace A.; Sekaly, Rafick; Baden, Lindsey R.; [...]
  • Erschienen: Springer Science and Business Media LLC, 2024
  • Erschienen in: Nature Communications, 15 (2024) 1
  • Sprache: Englisch
  • DOI: 10.1038/s41467-023-44211-0
  • ISSN: 2041-1723
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  • Anmerkungen:
  • Beschreibung: AbstractThe glycosylation of IgG plays a critical role during human severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection, activating immune cells and inducing cytokine production. However, the role of IgM N-glycosylation has not been studied during human acute viral infection. The analysis of IgM N-glycosylation from healthy controls and hospitalized coronavirus disease 2019 (COVID-19) patients reveals increased high-mannose and sialylation that correlates with COVID-19 severity. These trends are confirmed within SARS-CoV-2-specific immunoglobulin N-glycan profiles. Moreover, the degree of total IgM mannosylation and sialylation correlate significantly with markers of disease severity. We link the changes of IgM N-glycosylation with the expression of Golgi glycosyltransferases. Lastly, we observe antigen-specific IgM antibody-dependent complement deposition is elevated in severe COVID-19 patients and modulated by exoglycosidase digestion. Taken together, this work links the IgM N-glycosylation with COVID-19 severity and highlights the need to understand IgM glycosylation and downstream immune function during human disease.
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