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

Author

Listed:
  • 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)

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.

Suggested Citation

  • Theresa Kissel & Veerle F. A. M. Derksen & Arthur E. H. Bentlage & Carolien Koeleman & Lise Hafkenscheid & Diane Woude & Manfred Wuhrer & Gestur Vidarsson & René E. M. Toes, 2024. "N-linked Fc glycosylation is not required for IgG-B-cell receptor function in a GC-derived B-cell line," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-023-44468-5
    DOI: 10.1038/s41467-023-44468-5
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    References listed on IDEAS

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    1. Alexander D. Gitlin & Michel C. Nussenzweig, 2015. "Immunology: Fifty years of B lymphocytes," Nature, Nature, vol. 517(7533), pages 139-141, January.
    2. N. Giovannone & J. Liang & A. Antonopoulos & J. Geddes Sweeney & S. L. King & S. M. Pochebit & N. Bhattacharyya & G. S. Lee & A. Dell & H. R. Widlund & S. M. Haslam & C. J. Dimitroff, 2018. "Galectin-9 suppresses B cell receptor signaling and is regulated by I-branching of N-glycans," Nature Communications, Nature, vol. 9(1), pages 1-17, December.
    3. Niklas Engels & Lars M. König & Wiebke Schulze & Daniel Radtke & Kanika Vanshylla & Johannes Lutz & Thomas H. Winkler & Lars Nitschke & Jürgen Wienands, 2014. "The immunoglobulin tail tyrosine motif upgrades memory-type BCRs by incorporating a Grb2-Btk signalling module," Nature Communications, Nature, vol. 5(1), pages 1-11, December.
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