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

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)535-542
Number of pages8
JournalApplied Microbiology and Biotechnology
Issue number3
Publication statusPublished - 2010 Jan


  • Bispecific IgG-like antibody
  • Bispecific diabody
  • Chinese hamster ovary cells
  • Glycosylation
  • Immunoglobulin G

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology


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