The glycosylation profile of therapeutic glycoproteins is both an important and highly regulated product quality attribute. Glycosylation of protein biologics has been shown to be an impactful characteristic with respect to the pharmacokinetics and efficacy of these molecules. Specifically, impacts to the domain stability, higher order structure, and binding affinity of multiple therapeutic antibodies can be the result of changes in the glycosylation profile. Here, we present our findings that glycosylation levels of a novel bispecific immunoglobulin are linked to particular process parameters demonstrated during bioreactor culture. Our work to identify the root cause of this product quality attribute during development and subsequent GMP manufacturing of this molecule through upstream process optimization is demonstrated. We have provided a novel means to control with precision the uncommon product quality profile of this unique molecule, and to dramatically improve process robustness.

Identification and control of a unique glycosylation sensitivity in a bispecific immunoglobulin

253rd National Meeting (2017)

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