Production of Highly Sialylated Monoclonal Antibodies
Open accessAbstract
The first monoclonal antibody (Mab), developed against kidney transplant rejection, was accepted by the FDA in 1986 [1]. Today, Mabs are leading the biotherapeutics market as 28 have been approved in Europe and the USA, and hundreds are in clinical trials [2-4]. Most of them are of IgG1 subtype, developed for cancer and immune disease treatments. Mabs clinical efficacy not only relies on specific target binding provided by their variable region, but also on their ability to trigger defense mechanisms such as antibody-dependent cellular cytotoxicity (ADCC) and complement dependent cytotoxicity (CDC). These effector functions are mediated by the interaction between the antibody Fc fragment and the Fcγ-receptors expressed on immune cell surfaces or the molecules of the complement involved in ADCC and CDC respectively. In the last decade, these interactions were found to be highly dependent on on the presence and structure of the N-glycan linked to the Fc fragment [5, 6].
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Transient expression of ST6Gal1 in CHO and HEK293 cells also increased the α2,6 sialylation of a trastuzumab F243A mutant antibody.
“Transient expression of ST6Gal1 in CHO and HEK293 cells also increased the α2,6 sialylation of a trastuzumab F243A mutant antibody (Raymond et al., 2012).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Raymond et al., 2012
Section 4 describes transient coexpression of ST6Gal-I with trastuzumab in CHO and HEK293 cells, and the section on ST6Gal-I overexpression reports increased α2,6-sialylation of the mutant antibody. However, the trastuzumab mutant studied is F246A; the paper says it is equivalent to a previously described IgG3 F243A mutant, not that trastuzumab itself has the F243A mutation. (LLM, conf=0.90)
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Roy, R. (2017) · Mspace (University of Manitoba)
- Authors
- Raymond, C., Robotham, A. C., Kelly, J., Lattová, E., Perreault, H., & Durocher, Y.
- Affiliations
- National Research Council Canada (CA)
- Venue
- InTech eBooks
- Publisher
- InTech
- Published
- 2012-09-26
- OpenAlex
- W1544799888
- Cited by
- 20
- References
- 50
- Citations by year
- 2022: 1 · 2021: 3 · 2020: 3 · 2019: 2 · 2017: 3 · 2016: 2 · 2015: 4 · 2014: 2
- FWCI
- 6.46
- Type
- book chapter
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- InTech eBooks (publishedVersion, cc-by)
- Contact-less Assessment of In-vivo Body Signals Using Microwave Doppler Radar (InTech) (submittedVersion, cc-by)
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Keywords
- monoclonal antibodies, sialylation, Fc glycosylation, N-glycans, IgG1, antibody effector functions, antibody-dependent cellular cytotoxicity, complement-dependent cytotoxicity, Fc gamma receptor, biologic therapy
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