Nimmerjahn F (2025)
Publication Language: English
Publication Type: Book chapter / Article in edited volumes
Publication year: 2025
Publisher: Springer
Edited Volumes: Complex Carbohydrates in Health and Disease
Series: Handbook of Experimental Pharmacology
City/Town: Cham
Book Volume: 288
Pages Range: 189-209
ISBN: 978-3-032-02582-1
DOI: 10.1007/164_2025_744
Immunoglobulin G (IgG) antibodies are an essential component of humoral immunity protecting the host from recurrent infections. Among all antibody isotypes, IgG antibodies have a uniquely long half-life, can basically reach any tissue in the body, and have the ability to kill opsonized target cells, which has made them the molecule of choice for therapeutic interventions in cancer and autoimmunity. Moreover, IgG antibodies in the form of pooled serum IgG preparations from healthy donors are used to treat chronic inflammatory and autoimmune diseases, providing evidence that serum IgG antibodies can have an active immunomodulatory activity. Research over the last two decades has established that the single sugar moiety attached to each IgG heavy chain plays a very important role in modulating the pro- and anti-inflammatory activities of IgG. Moreover, specific sugar moieties such as sialic acid and galactose residues can serve as highly specific biomarkers for ongoing inflammatory processes. This chapter will summarize how different sugar residues in the IgG sugar moiety change upon inflammation and how such changes may translate to altered IgG function and hence maybe useful for optimizing or modulating the function of therapeutic antibodies.
APA:
Nimmerjahn, F. (2025). Role of Antibody Glycosylation in Health, Disease, and Therapy. In Fabian Pfrengle, Kevin Pagel, Rudolf Tauber (Eds.), Complex Carbohydrates in Health and Disease. (pp. 189-209). Cham: Springer.
MLA:
Nimmerjahn, Falk. "Role of Antibody Glycosylation in Health, Disease, and Therapy." Complex Carbohydrates in Health and Disease. Ed. Fabian Pfrengle, Kevin Pagel, Rudolf Tauber, Cham: Springer, 2025. 189-209.
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