iScience (Sep 2023)

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

  • 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,
  • Adam Sander,
  • David E. Schmidt,
  • Maurice Steenhuis,
  • Theo Rispens,
  • Morten A. Nielsen,
  • 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,
  • Niels van Mourik,
  • Sabine E. Olie,
  • Edgar J.G. Peters,
  • Tom D.Y. Reijnders,
  • Michiel Schinkel,
  • Alex R. Schuurman,
  • Jonne J. Sikkens,
  • Marleen A. Slim,
  • Yvo M. Smulders,
  • Alexander P.J. Vlaar,
  • Lonneke A. van Vught,
  • Joost W. Wiersinga,
  • Antinori Spinello,
  • Cinzia Bassoli,
  • Giovanna Bestetti,
  • Mario Corbellino,
  • Alice Covizzi,
  • Angelica Lupo,
  • Laura Milazzo,
  • Marco Schiuma,
  • Alessandro Torre,
  • Willem A. de Jongh,
  • Ali Salanti,
  • Thor G. Theander,
  • Matthew B.B. McCall,
  • Meral Esen

Journal volume & issue
Vol. 26, no. 9
p. 107619

Abstract

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Summary: 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.

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