N-linked Fc glycosylation is not required for IgG-B-cell receptor function in a GC-derived B-cell line

Theresa Kissel (), Veerle F. A. M. Derksen, Arthur E. H. Bentlage, Carolien Koeleman, Lise Hafkenscheid, Diane Woude, Manfred Wuhrer, Gestur Vidarsson and René E. M. Toes ()
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Theresa Kissel: Leiden University Medical Center
Veerle F. A. M. Derksen: Leiden University Medical Center
Arthur E. H. Bentlage: University of Amsterdam
Carolien Koeleman: Leiden University Medical Center
Lise Hafkenscheid: Leiden University Medical Center
Diane Woude: Leiden University Medical Center
Manfred Wuhrer: Leiden University Medical Center
Gestur Vidarsson: University of Amsterdam
René E. M. Toes: Leiden University Medical Center

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: Abstract IgG secreted by B cells carry asparagine N(297)-linked glycans in the fragment crystallizable (Fc) region. Changes in Fc glycosylation are related to health or disease and are functionally relevant, as IgG without Fc glycans cannot bind to Fcɣ receptors or complement factors. However, it is currently unknown whether ɣ-heavy chain (ɣHC) glycans also influence the function of membrane-bound IgG-B-cell receptors (BCR) and thus the outcome of the B-cell immune response. Here, we show in a germinal center (GC)-derived human B-cell line that ɣHC glycans do not affect membrane expression of IgG-BCRs. Furthermore, antigen binding or other BCR-facilitated mechanisms appear unaffected, including BCR downmodulation or BCR-mediated signaling. As expected, secreted IgG lacking Fc glycosylation is unable to carry out effector functions. Together, these observations indicate that IgG-Fc glycosylation serves as a mechanism to control the effector functions of antibodies, but does not regulate the activation of IgG-switched B cells, as its absence had no apparent impact on BCR function.

Date: 2024
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DOI: 10.1038/s41467-023-44468-5

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