tetano
Editor, Senior Moderator
Nat Commun
. 2024 Jan 9;15(1):404.
doi: 10.1038/s41467-023-44211-0. IgM N-glycosylation correlates with COVID-19 severity and rate of complement deposition
Benjamin S Haslund-Gourley[SUP] 1 [/SUP], Kyra Woloszczuk[SUP] 1 [/SUP], Jintong Hou[SUP] 1 [/SUP], Jennifer Connors[SUP] 1 [/SUP], Gina Cusimano[SUP] 1 [/SUP], Mathew Bell[SUP] 1 [/SUP], Bhavani Taramangalam[SUP] 1 [/SUP], Slim Fourati[SUP] 2 [/SUP], Nathan Mege[SUP] 1 [/SUP], Mariana Bernui[SUP] 1 [/SUP], Matthew C Altman[SUP] 3 [/SUP], Florian Krammer[SUP] 4 5 6 [/SUP], Harm van Bakel[SUP] 4 5 6 [/SUP]; IMPACC Network; Holden T Maecker[SUP] 7 [/SUP], Nadine Rouphael[SUP] 2 [/SUP], Joann Diray-Arce[SUP] 8 [/SUP], Brian Wigdahl[SUP] 1 [/SUP], Michele A Kutzler[SUP] 1 [/SUP], Charles B Cairns[SUP] 1 [/SUP], Elias K Haddad[SUP] 9 [/SUP], Mary Ann Comunale[SUP] 10 [/SUP]
Collaborators, Affiliations
The 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.
. 2024 Jan 9;15(1):404.
doi: 10.1038/s41467-023-44211-0. IgM N-glycosylation correlates with COVID-19 severity and rate of complement deposition
Benjamin S Haslund-Gourley[SUP] 1 [/SUP], Kyra Woloszczuk[SUP] 1 [/SUP], Jintong Hou[SUP] 1 [/SUP], Jennifer Connors[SUP] 1 [/SUP], Gina Cusimano[SUP] 1 [/SUP], Mathew Bell[SUP] 1 [/SUP], Bhavani Taramangalam[SUP] 1 [/SUP], Slim Fourati[SUP] 2 [/SUP], Nathan Mege[SUP] 1 [/SUP], Mariana Bernui[SUP] 1 [/SUP], Matthew C Altman[SUP] 3 [/SUP], Florian Krammer[SUP] 4 5 6 [/SUP], Harm van Bakel[SUP] 4 5 6 [/SUP]; IMPACC Network; Holden T Maecker[SUP] 7 [/SUP], Nadine Rouphael[SUP] 2 [/SUP], Joann Diray-Arce[SUP] 8 [/SUP], Brian Wigdahl[SUP] 1 [/SUP], Michele A Kutzler[SUP] 1 [/SUP], Charles B Cairns[SUP] 1 [/SUP], Elias K Haddad[SUP] 9 [/SUP], Mary Ann Comunale[SUP] 10 [/SUP]
Collaborators, Affiliations
- PMID: 38195739
- PMCID: PMC10776791
- DOI: 10.1038/s41467-023-44211-0
The 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.