The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
General mechanism for modulating immunoglobulin effector function
Open accessAbstract
Immunoglobulins recognize and clear microbial pathogens and toxins through the coupling of variable region specificity to Fc-triggered cellular activation. These proinflammatory activities are regulated, thus avoiding the pathogenic sequelae of uncontrolled inflammation by modulating the composition of the Fc-linked glycan. Upon sialylation, the affinities for Fcγ receptors are reduced, whereas those for alternative cellular receptors, such as dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN)/CD23, are increased. We demonstrate that sialylation induces significant structural alterations in the Cγ2 domain and propose a model that explains the observed changes in ligand specificity and biological activity. By analogy to related complexes formed by IgE and its evolutionarily related Fc receptors, we conclude that this mechanism is general for the modulation of antibody-triggered immune responses, characterized by a shift between an “open” activating conformation and a “closed” anti-inflammatory state of antibody Fc fragments. This common mechanism has been targeted by pathogens to avoid host defense and offers targets for therapeutic intervention in allergic and autoimmune disorders.
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Citations
Cites
Anti-Inflammatory Activity of Immunoglobulin G Resulting from Fc Sialylation
Kaneko, Y., Nimmerjahn, F., & Ravetch, J. V. (2006) · Science · doi:10.1126/science.1129594 · Cited by 1,754
Self-citationRecapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc
Anthony, R. M., Nimmerjahn, F., Ashline, D. J., Reinhold, V. N., Paulson, J. C., & Ravetch, J. V. (2008) · Science · doi:10.1126/science.1154315 · Cited by 849
Self-citationRole of Oligosaccharide Residues of IgG1-Fc in FcγRIIb Binding
Mimura, Y., Sondermann, P., Ghirlando, R., Lund, J., Young, S. P., Goodall, M., & Jefferis, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107478200 · Cited by 236
Self-citation
Cited by
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
“More recent evidence suggests that the Fcregion of other Ig classes may also alter effector function (709, 710).”
BackgroundIgG Subclasses and Allotypes: From Structure to Effector Functions
Vidarsson, G., Dekkers, G., & Rispens, T. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00520 · Cited by 2,667
Liu, L. (2015) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.24444 · Cited by 428
The Immunoregulatory Roles of Antibody Glycosylation
Jennewein, M. F., & Alter, G. (2017) · Trends in Immunology · doi:10.1016/j.it.2017.02.004 · Cited by 323
Sialylation of IgG Fc domain impairs complement-dependent cytotoxicity
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) · Journal of Clinical Investigation · doi:10.1172/jci82695 · Cited by 269
Metadata
- Authors
- Sondermann, P., Pincetic, A., Maamary, J., Lammens, K., & Ravetch, J. V.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2013-05-22
- Volume
- 110
- Issue
- 24
- Pages
- 9868-9872
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2037117519
- Cited by
- 218
- References
- 3
- FWCI
- 18.30
- Type
- journal article
- Language
- en
- Open access
- green
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