The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Enhancing Antibody Fc Heterodimer Formation through Electrostatic Steering Effects
Open accessAbstract
Naturally occurring IgG antibodies are bivalent and monospecific. Bispecific antibodies having binding specificities for two different antigens can be produced using recombinant technologies and are projected to have broad clinical applications. However, co-expression of multiple light and heavy chains often leads to contaminants and pose purification challenges. In this work, we have modified the CH3 domain interface of the antibody Fc region with selected mutations so that the engineered Fc proteins preferentially form heterodimers. These novel mutations create altered charge polarity across the Fc dimer interface such that coexpression of electrostatically matched Fc chains support favorable attractive interactions thereby promoting desired Fc heterodimer formation, whereas unfavorable repulsive charge interactions suppress unwanted Fc homodimer formation. This new Fc heterodimer format was used to produce bispecific single chain antibody fusions and monovalent IgGs with minimal homodimer contaminants. The strategy proposed here demonstrates the feasibility of robust production of novel Fc-based heterodimeric molecules and hence broadens the scope of bispecific molecules for therapeutic applications.
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Cites
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Cited by
Bispecific antibodies: a mechanistic review of the pipeline
Labrijn, A. F., Janmaat, M. L., Reichert, J. M., & Parren, P. W. H. I. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0028-1 · Cited by 1,303
Alternative molecular formats and therapeutic applications for bispecific antibodies
Spiess, C., Zhai, Q., & Carter, P. J. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.01.003 · Cited by 607
Kontermann, R. E., & Brinkmann, U. (2015) · Drug Discovery Today · doi:10.1016/j.drudis.2015.02.008 · Cited by 578
Efficient generation of stable bispecific IgG1 by controlled Fab-arm exchange
Labrijn, A. F., Meesters, J. I., de Goeij, B. E. C. G., van den Bremer, E. T. J., Neijssen, J., van Kampen, M. D., Strumane, K., Verploegen, S., Kundu, A., Gramer, M. J., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220145110 · Cited by 339
A bispecific antibody targeting sclerostin and DKK-1 promotes bone mass accrual and fracture repair
Florio, M., Gunasekaran, K., Stolina, M., Li, X., Liu, L., Tipton, B., Salimi-Moosavi, H., Asuncion, F. J., Li, C., Sun, B., et al. (2016) · Nature Communications · doi:10.1038/ncomms11505 · Cited by 257
Self-citation
Metadata
- Authors
- Gunasekaran, K., Pentony, M., Shen, M., Garrett, L., Forte, C., Woodward, A., Ng, S. B., Born, T., Retter, M., Manchulenko, K., Sweet, H., Foltz, I. N., Wittekind, M., & Yan, W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-06
- Volume
- 285
- Issue
- 25
- Pages
- 19637-19646
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2021855052
- Cited by
- 280
- References
- 32
- FWCI
- 10.61
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Gunasekaran, K., Pentony, M., Shen, M., Garrett, L., Forte, C., Woodward, A., Ng, S. B., Born, T., Retter, M., Manchulenko, K., Sweet, H., Foltz, I. N., Wittekind, M., & Yan, W. (2010). Enhancing Antibody Fc Heterodimer Formation through Electrostatic Steering Effects. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m110.117382
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