One of the most important structural features of recombinant monoclonal antibodies produced in mammalian cells is the N-linked oligosaccharide profile. These profiles impact recombinant therapeutics in a multitude of ways affecting distribution, efficacy, and immunogenicity. High mannose, alpha-gal and other oligosaccharide species are highly immunogenic and in most cases should be minimized during manufacturing. A recombinant monoclonal antibody, h5G1.1, was produced in NS0 and CHO cell lines and tested to identify changes in the N-linked oligosaccharide profiles caused from a change in cell line. Traditional peak analysis using HPLC with fluorescence detection was augmented by mass spectrometric analysis. Nano LC-MS following tryptic digestion corroborated HPLC findings of the presence of several alpha-gal oligosaccharide species in the recombinant IgG (rIgG) from NS0 cell line. Both cell lines possessed rIgGs with complex and small amounts of high mannose glycans.
CITATION STYLE
Kilgore, B. R., Lucka, A. W., Patel, R., Andrien, B. A., & Dhume, S. T. (2008). Comparability and Monitoring Immunogenic N-linked Oligosaccharides from Recombinant Monoclonal Antibodies from Two Different Cell Lines using HPLC with Fluorescence Detection and Mass Spectrometry. In Post-translational Modifi cations of Proteins (pp. 333–346). Humana Press. https://doi.org/10.1007/978-1-60327-084-7_23
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