On the achievable consistency of glycan distribution in biomanufacturing of therapeutic mAbs
Hongbin Zhu, Joshua Shipman, Weiming Ouyang, Kang Chen
TL;DR
This study shows that the glycan profiles of monoclonal antibody drugs remain consistent enough across batches to not affect their safety or effectiveness.
Contribution
The study quantifies glycan variation in therapeutic mAbs over time, showing it remains within safe and consistent ranges.
Findings
Glycan relative abundance varied by up to 4% across lots of trastuzumab and adalimumab.
ANOVA detected a ~1% drift in glycan profiles, which is unlikely to impact drug safety or efficacy.
Modern manufacturing processes can maintain glycan consistency within achievable ranges.
Abstract
Recombinant monoclonal antibody (mAb) therapeutics exhibit lot-to-lot glycosylation variation influenced by manufacturing processes, which remains underexplored publicly. This study analyzed five years of trastuzumab and adalimumab lots, revealing up to 4% range of variation in glycan relative abundance and significant change or drift of ~1% by ANOVA, levels unlikely to affect mAb efficacy or safety. The results suggest that modern manufacturing can maintain consistent glycan profiles within realistically achievable ranges.
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Taxonomy
TopicsViral Infectious Diseases and Gene Expression in Insects · Monoclonal and Polyclonal Antibodies Research · Protein purification and stability