Glycosylation analysis of an aggregated antibody produced by Chinese hamster ovary cells in bioreactor culture

Masayoshi Onitsuka, Akira Kawaguchi, Ryutaro Asano, Izumi Kumagai, Kohsuke Honda, Hisao Ohtake, Takeshi Omasa

研究成果: Article査読

15 被引用数 (Scopus)

抄録

N-Glycosylation of therapeutic antibodies contributes not only to their biological function, but also to their stability and tendency to aggregate. Here, we investigated the impact of the glycosylation status of an aggregated antibody that accumulated during the bioreactor culture of Chinese hamster ovary cells. High-performance liquid chromatography analysis showed that there was no apparent difference in the glycosylation patterns of monomeric, dimeric, and large aggregated forms of the antibody. In contrast, lectin binding assays, which enable the total amounts of specific sugar residues to be detected, showed that both galactose and fucose residues in dimers and large aggregates were reduced to 70-80% of the amount in monomers. These results strongly suggest that the lack of N-linked oligosaccharides, a result of deglycosylation or aglycosylation, occurred in a proportion of the dimeric and large aggregated components. The present study demonstrates that glycosylation heterogeneities are a potential cause of antibody aggregation in cell culture of Chinese hamster ovary cells, and that the lack of N-glycosylation promotes the formation of dimers and finally results in large aggregates.

本文言語English
ページ(範囲)639-644
ページ数6
ジャーナルJournal of Bioscience and Bioengineering
117
5
DOI
出版ステータスPublished - 2014 5

ASJC Scopus subject areas

  • バイオテクノロジー
  • バイオエンジニアリング
  • 応用微生物学とバイオテクノロジー

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