IgM N-glycosylation correlates with COVID-19 severity and rate of complement deposition

Bibliographic Details
Title: IgM N-glycosylation correlates with COVID-19 severity and rate of complement deposition
Authors: Benjamin S. Haslund-Gourley, Kyra Woloszczuk, Jintong Hou, Jennifer Connors, Gina Cusimano, Mathew Bell, Bhavani Taramangalam, Slim Fourati, Nathan Mege, Mariana Bernui, Matthew C. Altman, Florian Krammer, Harm van Bakel, IMPACC Network, Holden T. Maecker, Nadine Rouphael, Joann Diray-Arce, Brian Wigdahl, Michele A. Kutzler, Charles B. Cairns, Elias K. Haddad, Mary Ann Comunale
Source: Nature Communications, Vol 15, Iss 1, Pp 1-19 (2024)
Publisher Information: Nature Portfolio, 2024.
Publication Year: 2024
Collection: LCC:Science
Subject Terms: Science
More Details: Abstract 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.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2041-1723
Relation: https://doaj.org/toc/2041-1723
DOI: 10.1038/s41467-023-44211-0
Access URL: https://doaj.org/article/3ec94a3f579544858deda0f8801d626a
Accession Number: edsdoj.3ec94a3f579544858deda0f8801d626a
Database: Directory of Open Access Journals
More Details
ISSN:20411723
DOI:10.1038/s41467-023-44211-0
Published in:Nature Communications
Language:English