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        New Enzymatic Workflows for Analysis of O-Glycosylated Biopharmaceuticals

        O-glycosylation is a difficult post-translational modification to analyze. The heterogeneity of O-glycosylation can make MS analysis difficult. Currently, there is a growing interest in this type of glycosylation and a need for new tools. The OglyZOR enzyme is an O-glycosidase able to remove O-glycans from proteins under native conditions. Paired with PNGase F, a total deglycosylation of complex biopharmaceuticals can be achieved by middle-level MS.

        OpeRATOR is protease that binds to O-glycosylated proteins and digests the protein backbone N-terminally to the glycosylated serine or threonine residues. OpeRATOR can be used to generate O-glycopeptides which can be analyzed by LC-MS for in-depth mapping of O-glycosylation sites and quantitative comparisons of O-glycosylation patterns in biopharmaceuticals.

        About the presenter

        Andreas Naegeli, Senior Scientist, Genovis

        Andreas Naegeli, Senior Scientist, Genovis

        Andreas did his PhD with Prof. Markus Aebi at ETH Zurich in Switzerland where he studied bacterial glycosylation systems and their biotechnological and medical applications. He finished in 2014 and moved to Lund, Sweden for a postdoctoral research position where he used targeted proteomics approaches to study changes in antibody glycosylation during bacterial infections. Since June 2018, he has been working at Genovis as a senior scientist in application development.

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