Sweet Rules: Linking Glycosylation to Antibody Function

Nimmerjahn F, Werner A (2021)

Publication Type: Book chapter / Article in edited volumes

Publication year: 2021

Edited Volumes: Antibody Glycosylation

Series: Experientia Supplementum

Book Volume: 112

Pages Range: 365-393

ISBN: 978-3-030-76911-6

DOI: 10.1007/978-3-030-76912-3_12


Antibodies produced upon infections with pathogenic microorganisms are essential for clearing primary infections and for providing the host with long-lasting immunity. Moreover, antibodies have become the most widely used platform for developing novel therapies against cancer and autoimmunity, requiring an in-depth understanding of how antibodies mediate their activity in vivo and which factors modulate pro- or anti-inflammatory antibody activities. Since the discovery that select residues present in the sugar domain attached to the immunoglobulin G (IgG) fragment crystallizable (Fc) region can modulate both, pro- and anti-inflammatory effector functions, a wealth of studies has focused on understanding how IgG glycosylation is regulated and how this knowledge can be used to optimize therapeutic antibody activity. With the introduction of glycoengineered afucosylated antibodies in cancer therapy and the initiation of clinical testing of highly sialylated anti-inflammatory antibodies the proof-of-concept that understanding antibody glycosylation can lead to clinical innovation has been provided. The focus of this review is to summarize recent insights into how antibody glycosylation is regulated in vivo and how select sugar residues impact IgG function.

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How to cite


Nimmerjahn, F., & Werner, A. (2021). Sweet Rules: Linking Glycosylation to Antibody Function. In Marija Pezer (Eds.), Antibody Glycosylation. (pp. 365-393).


Nimmerjahn, Falk, and Anja Werner. "Sweet Rules: Linking Glycosylation to Antibody Function." Antibody Glycosylation. Ed. Marija Pezer, 2021. 365-393.

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