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

Author

Listed:
  • Benjamin S. Haslund-Gourley

    (Drexel University/Tower Health Hospital)

  • Kyra Woloszczuk

    (Drexel University/Tower Health Hospital)

  • Jintong Hou

    (Drexel University/Tower Health Hospital)

  • Jennifer Connors

    (Drexel University/Tower Health Hospital)

  • Gina Cusimano

    (Drexel University/Tower Health Hospital)

  • Mathew Bell

    (Drexel University/Tower Health Hospital)

  • Bhavani Taramangalam

    (Drexel University/Tower Health Hospital)

  • Slim Fourati

    (Emory University)

  • Nathan Mege

    (Drexel University/Tower Health Hospital)

  • Mariana Bernui

    (Drexel University/Tower Health Hospital)

  • Matthew C. Altman

    (Benaroya Research Institute)

  • Florian Krammer

    (Department of Microbiology, Icahn School of Medicine at Mount Sinai
    Molecular and Cell Based Medicine, Icahn School of Medicine at Mount Sinai
    Center for Vaccine Research and Pandemic Preparedness (C-VaRPP), Icahn School of Medicine at Mount Sinai)

  • Harm Bakel

    (Department of Microbiology, Icahn School of Medicine at Mount Sinai
    Molecular and Cell Based Medicine, Icahn School of Medicine at Mount Sinai
    Center for Vaccine Research and Pandemic Preparedness (C-VaRPP), Icahn School of Medicine at Mount Sinai)

  • Holden T. Maecker

    (Stanford University)

  • Nadine Rouphael

    (Emory University)

  • Joann Diray-Arce

    (Clinical & Data Coordinating Center (CDCC); Precision Vaccines Program, Boston Children’s Hospital)

  • Brian Wigdahl

    (Drexel University/Tower Health Hospital)

  • Michele A. Kutzler

    (Drexel University/Tower Health Hospital)

  • Charles B. Cairns

    (Drexel University/Tower Health Hospital)

  • Elias K. Haddad

    (Drexel University/Tower Health Hospital)

  • Mary Ann Comunale

    (Drexel University/Tower Health Hospital)

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.

Suggested Citation

  • 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 & , 2024. "IgM N-glycosylation correlates with COVID-19 severity and rate of complement deposition," Nature Communications, Nature, vol. 15(1), pages 1-19, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-023-44211-0
    DOI: 10.1038/s41467-023-44211-0
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    1. Wenhui Li & Michael J. Moore & Natalya Vasilieva & Jianhua Sui & Swee Kee Wong & Michael A. Berne & Mohan Somasundaran & John L. Sullivan & Katherine Luzuriaga & Thomas C. Greenough & Hyeryun Choe & M, 2003. "Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus," Nature, Nature, vol. 426(6965), pages 450-454, November.
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