The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
Sialylation of IgG Fc domain impairs complement-dependent cytotoxicity
Open accessAbstract
IgG molecules exert both pro- and antiinflammatory effector functions based on the composition of the fragment crystallizable (Fc) domain glycan. Sialylated IgG Fc domains have antiinflammatory properties that are attributed to their ability to increase the activation threshold of innate effector cells to immune complexes by stimulating the upregulation of the inhibitory Fcγ receptor IIB (FcγRIIB). Here, we report that IgG Fc sialylation of human monoclonal IgG1 molecules impairs their efficacy to induce complement-mediated cytotoxicity (CDC). Fc sialylation of a CD20-targeting antibody had no impact on antibody-dependent cellular cytotoxicity and did not change the affinity of the antibody for activating Fcγ receptors. In contrast, the presence of sialic acid abrogated the increased binding of C1q to Fc-galactosylated IgG1 and resulted in decreased levels of C3b deposition on the cell surface. Similar to monoclonal antibodies, sialic acid inhibited the increased C1q binding to galactosylated Fc fragments in human polyclonal IgG. In sera derived from patients with chronic inflammatory demyelinating polyneuropathy, an autoimmune disease of the peripheral nervous system in which humoral immune responses mediate tissue damage, induction of IgG Fc sialylation was associated with clinical disease remission. Thus, impairment of CDC represents an FcγR-independent mechanism by which Fc-sialylated glycovariants might limit proinflammatory IgG effector functions.
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Cites
Anti-Inflammatory Activity of Immunoglobulin G Resulting from Fc Sialylation
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Self-citationThe Impact of Glycosylation on the Biological Function and Structure of Human Immunoglobulins
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Divergent Immunoglobulin G Subclass Activity Through Selective Fc Receptor Binding
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Self-citationFcR γ chain deletion results in pleiotrophic effector cell defects
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Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc
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Self-citationIntravenous immunoglobulin therapy: how does IgG modulate the immune system?
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Cited by
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
Glycosylation in health and disease
Reily, C., Stewart, T. J., Renfrow, M. B., & Novak, J. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0129-4 · Cited by 2,075
Antibody glycoengineering strategies in mammalian cells
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Chung, C., Wang, Q., Yang, S., Ponce, S. A., Kirsch, B. J., Zhang, H., & Betenbaugh, M. J. (2017) · Biotechnology and Bioengineering · doi:10.1002/bit.26375 · Cited by 32
Bheemareddy, B. R., Pulipeta, M., Iyer, P., & Dirisala, V. R. (2019) · Journal of Carbohydrate Chemistry · doi:10.1080/07328303.2018.1541995 · Cited by 7
Metadata
- Authors
- Quast, I., Keller, C. W., Maurer, M. A., Giddens, J. P., Tackenberg, B., Wang, L.-X., Münz, C., Nimmerjahn, F., Dalakas, M. C., & Lünemann, J. D.
- Venue
- Journal of Clinical Investigation
- Published
- 2015-10-05
- Volume
- 125
- Issue
- 11
- Pages
- 4160-4170
- ISSN
- 0021-9738 (ISSN-L)
- 1558-8238
- OpenAlex
- W1874142858
- Cited by
- 269
- References
- 57
- FWCI
- 9.26
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Quast, I., Keller, C. W., Maurer, M. A., Giddens, J. P., Tackenberg, B., Wang, L.-X., Münz, C., Nimmerjahn, F., Dalakas, M. C., & Lünemann, J. D. (2015). Sialylation of IgG Fc domain impairs complement-dependent cytotoxicity. Journal of Clinical Investigation. https://doi.org/10.1172/jci82695
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