Comparative analysis of spike-specific IgG Fc glycoprofiles elicited by adenoviral, mRNA, and protein-based SARS-CoV-2 vaccines

Research output: Contribution to journalJournal articleResearchpeer-review


  • Fulltext

    Final published version, 4.29 MB, PDF document

  • Julie Van Coillie
  • Tamas Pongracz
  • Tonći Šuštić
  • Wenjun Wang
  • Jan Nouta
  • Mathieu Le Gars
  • Sofie Keijzer
  • Federica Linty
  • Olvi Cristianawati
  • Jim B.D. Keijser
  • Remco Visser
  • Lonneke A. van Vught
  • Marleen A. Slim
  • Niels van Mourik
  • Merel J. Smit
  • Bertelsen, Adam Frederik Sander
  • David E. Schmidt
  • Maurice Steenhuis
  • Theo Rispens
  • Nielsen, Morten Agertoug
  • Benjamin G. Mordmüller
  • Alexander P.J. Vlaar
  • C. Ellen van der Schoot
  • Ramon Roozendaal
  • Manfred Wuhrer
  • Gestur Vidarsson
  • Brent Appelman
  • Diederik van de Beek
  • Marije K. Bomers
  • Justin de Brabander
  • Matthijs C. Brouwer
  • David T.P. Buis
  • Nora Chekrouni
  • Marit J. van Gils
  • Menno D. de Jong
  • Ayesha H.A. Lavell
  • Sabine E. Olie
  • Edgar J.G. Peters
  • Tom D.Y. Reijnders
  • Michiel Schinkel
  • Alex R. Schuurman
  • Jonne J. Sikkens
  • Yvo M. Smulders
  • Joost W. Wiersinga
  • Antinori Spinello
  • Cinzia Bassoli
  • Giovanna Bestetti
  • Mario Corbellino
  • Salanti, Ali
  • Theander, Thor Grundtvig
  • in collaboration with the UMC COVID-19 S3/HCW study group

IgG antibodies are important mediators of vaccine-induced immunity through complement- and Fc receptor-dependent effector functions. Both are influenced by the composition of the conserved N-linked glycan located in the IgG Fc domain. Here, we compared the anti-Spike (S) IgG1 Fc glycosylation profiles in response to mRNA, adenoviral, and protein-based COVID-19 vaccines by mass spectrometry (MS). All vaccines induced a transient increase of antigen-specific IgG1 Fc galactosylation and sialylation. An initial, transient increase of afucosylated IgG was induced by membrane-encoding S protein formulations. A fucose-sensitive ELISA for antigen-specific IgG (FEASI) exploiting FcγRIIIa affinity for afucosylated IgG was used as an orthogonal method to confirm the LC-MS-based afucosylation readout. Our data suggest that vaccine-induced anti-S IgG glycosylation is dynamic, and although variation is seen between different vaccine platforms and individuals, the evolution of glycosylation patterns display marked overlaps.

Original languageEnglish
Article number107619
Issue number9
Pages (from-to)1-15
Publication statusPublished - 2023

Bibliographical note

Publisher Copyright:
© 2023 The Author(s)

    Research areas

  • Glycomics, Immune response, Immunology, Microbiology

Number of downloads are based on statistics from Google Scholar and

No data available

ID: 373870913