作者
Julie Van Coillie, Tamas Pongracz, Tonći Šuštić, Wenjun Wang, Jan Nouta, Mathieu Le Gars, Sofie Keijzer, Federica Linty, Olvi Cristianawati, Jim BD 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 PJ 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 TP Buis, Nora Chekrouni, Marit J van Gils, Menno D de Jong, Ayesha HA Lavell, Sabine E Olie, Edgar JG Peters, Tom DY Reijnders, Michiel Schinkel, Alex R Schuurman, Jonne J Sikkens, Yvo M Smulders, 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 BB McCall, Meral Esen
发表日期
2023/9/15
期刊
Iscience
卷号
26
期号
9
出版商
Elsevier
简介
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 …
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J Van Coillie, T Pongracz, T Šuštić, W Wang, J Nouta… - Iscience, 2023