The DOI matches its Crossref record; 89 of the 89 references it cites were found in a registry or an index.
Antibody therapeutics: isotype and glycoform selection
Abstract
Recombinant monoclonal antibody (rMAb) therapy may be instituted to achieve one of two broad outcomes: i) killing of cells or organisms (e.g., cancer cells, bacteria); and ii) neutralisation of soluble molecules (e.g., cytokines in chronic disease or toxins in infection). The choice of rMAb isotype is a critical decision in the development of a therapeutic antibody as it will determine the biological activities triggered in vivo. It is not possible, however, to accurately predict the in vivo activity because multiple parameters impact on the functional outcome, for example, IgG subclass, IgG-Fc glycoform, epitope density, cellular Fc receptors polymorphisms and so on. The present understanding of the molecular interactions between IgG-Fc and effector ligands in vitro has allowed the generation of new antibody structures with altered/improved effector function profiles that may prove optimal for given disease indications. Thus, when maximal antibody-dependent cell-mediated cytotoxicity activity is indicated a non-fucosylated IgG1 format may be optimal; when minimal activity is indicated an aglycosylated IgG2 may be the form of choice.
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Cites
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Carter, P. J. (2006) · Nature Reviews Immunology · doi:10.1038/nri1837 · Cited by 1,099
Fcγ Receptors: Old Friends and New Family Members
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Engineered antibody Fc variants with enhanced effector function
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Cited by
Bruhns, P., Iannascoli, B., England, P., Mancardi, D. A., Fernandez, N., Jorieux, S., & Daëron, M. (2009) · Blood · doi:10.1182/blood-2008-09-179754 · Cited by 1,479
Glycosylation as a strategy to improve antibody-based therapeutics
Jefferis, R. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2804 · Cited by 829
Self-citationImmunogenicity to Biotherapeutics – The Role of Anti-drug Immune Complexes
Krishna, M., & Nadler, S. G. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00021 · Cited by 389
Alt, N., Zhang, T. Y., Motchnik, P., Taticek, R., Quarmby, V., Schlothauer, T., Beck, H., Emrich, T., & Harris, R. J. (2016) · Biologicals · doi:10.1016/j.biologicals.2016.06.005 · Cited by 294
Structural and Functional Characterization of Disulfide Isoforms of the Human IgG2 Subclass
Dillon, T. M., Ricci, M. S., Vezina, C., Flynn, G. C., Liu, Y. D., Rehder, D. S., Plant, M., Henkle, B., Li, Y., Deechongkit, S., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709988200 · Cited by 291
Metadata
- Authors
- Jefferis, R.
- Venue
- Expert Opinion on Biological Therapy
- Publisher
- Informa UK Limited
- Published
- 2007-08-29
- Volume
- 7
- Issue
- 9
- Pages
- 1401-1413
- ISSN
- 1471-2598 (ISSN-L)
- 1744-7682
- OpenAlex
- W2075219903
- Cited by
- 294
- References
- 89
- FWCI
- 14.59
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
