Glycosylation pattern of humanized IgG-like bispecific antibody produced by recombinant CHO cells

Wook Dong Kim, Miwako Tokunaga, Hiroyuki Ozaki, Takuya Ishibashi, Kohsuke Honda, Hiroyuki Kajiura, Kazuhito Fujiyama, Ryutaro Asano, Izumi Kumagai, Takeshi Omasa, Hisao Ohtake

研究成果: Article査読

20 被引用数 (Scopus)

抄録

The glycosylation pattern of a humanized anti-EGFR×anti-CD3 bispecific single-chain diabody with an Fc portion (hEx3-scDb-Fc) produced by recombinant Chinese hamster ovary cells was evaluated and compared with those of a recombinant humanized anti-IL-8 antibody (IgG1) and human serum IgG. N-Linked oligosaccharide structures were estimated by two-dimensional high-performance liquid chromatography and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. No sialylation was observed with purified hEx3-scDb-Fc and the anti-IL-8 antibody. From the analysis of neutral oligosaccharides, approximately more than 90% of the N-linked oligosaccharides of hEx3-scDb-Fc and the anti-IL-8 antibody were alpha-1,6-fucosylated. The galactosylated biantennary oligosaccharides comprise over 40% of the total N-linked oligosaccharides in both hEx3-scDb-Fc and the anti-IL-8 antibody. The fully galactosylated biantennary oligosaccharides from hEx3-scDb-Fc and the anti-IL-8 antibody accounted for only 10% of the N-linked; however, more than 20% of the N-linked oligosaccharides were fully galactosylated biantennary oligosaccharides in human serum IgG. The glycosylation pattern of hEx3-scDb-Fc was quite similar to that of the anti-IL-8 antibody.

本文言語English
ページ(範囲)535-542
ページ数8
ジャーナルApplied Microbiology and Biotechnology
85
3
DOI
出版ステータスPublished - 2010 1月

ASJC Scopus subject areas

  • バイオテクノロジー
  • 応用微生物学とバイオテクノロジー

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