Abstract
Monoclonal antibodies (mAbs) are amazingly successful in treating diseases such as various types of cancers, immune disorders, and infections. Currently, mAbs are considered the most versatile therapeutic available. Seminal scientific progress over the last decade on elucidating the functional role of antibody N-glycosylation revealed the significance of this post-translational modification on the stability, half-life, and biological activity of antibodies. Therefore, antibody N-glycosylation became a key aspect of biopharmaceutical mAb production in large-scale manufacturing processes. This Mini-Review summarizes the recent scientific attempts of producing mAbs in glycoengineered animal-, plant-, and yeast cell lines. Furthermore, we also describe novel approaches for analyzing mAb N-glycosylation.
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