Glycosylation as a strategy to improve antibody-based therapeutics
By R. Jefferis. Nature reviews. Drug discovery, 2009
838 citations recorded by the source corpus.
To date, more than 20 recombinant immunoglobulin G (IgG) antibody therapeutics are licensed for the treatment of various diseases. The mechanism of action of recombinant monoclonal antibodies (rMAbs) has been extensively investigated and several distinct pathways have been defined; selective activation of specific pathways may optimize clinical outcomes for different diseases, such as cancer and chronic inflammation. Human IgG is a glycoprotein with oligosaccharides attached at a single site. These are essential to the mode of action of rMAbs, and the antibody efficacy can vary depending on the particular oligosaccharide that is attached. Methods are now becoming available that allow the production of rMAbs bearing pre-selected oligosaccharides — glycoforms — to provide maximum efficacy for a given disease indication. This Review summarizes current knowledge of these methods and avenues for their exploitation in the clinic.
Subfields: Genetics, Molecular Biology, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/7e3a7d1cb9ba7fa0bf412272e3e97e1c2d8c9aa3
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Citations in the corpus
- Therapeutic antibodies for autoimmunity and inflammation (2010, methodology): “A second widely applicable and comparably successful method for increasing the IgG ADCC activity is through tailoring of Fc glycosylatio”
- Strategies and challenges for the next generation of therapeutic antibodies (2010, background): “, and the associated properties of the Fc can also be modulated by engineering at several levels: altering the glycosylation status to regulate anti- and pro-inflammatory propertie”
- Antibody Structure and Function: The Basis for Engineering Therapeutics (2019, background): “Likewise, glycosylation patterns can impact both PK and PD significantly [259,260].”