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PEDS Advance Access originally published online on July 11, 2008
Protein Engineering Design and Selection 2008 21(10):597-603; doi:10.1093/protein/gzn037
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© The Author 2008. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Preferential heterodimerization of a bispecific diabody based on a humanized anti-EGFR antibody 528

Ryutaro Asano1, Yukiko Sone1, Keiko Ikoma1, Hiroki Hayashi2, Takeshi Nakanishi1, Mitsuo Umetsu1, Yu Katayose2, Michiaki Unno2, Toshio Kudo3 and Izumi Kumagai1,4

1Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Sendai 980-8579 2Division of Gastroenterological Surgery, Department of Surgery, Graduate School of Medicine, Tohoku University, Sendai 980-8574 3Cell Resource Center for Biomedical Research, Institute of Development, Aging, and Cancer, Tohoku University, Sendai 980-8575, Japan

4 To whom correspondence should be addressed. E-mail: kmiz{at}kuma.che.tohoku.ac.jp

We report the utility of in vitro refolding in the preparation of monomorphous hEx3 bispecific diabodies with epidermal growth factor receptor and CD3 retargeting from insoluble aggregates in Escherichia coli. Appropriate interaction between cognate variable heavy and light chains led to the formation of functional hEx3 heterodimers in a diabody format rather than inactive homodimers. The refolded hEx3 was found to exhibit almost the equivalent activity to the hEx3 and single-chain hEx3 (hEx3-scDb) prepared in a mammalian secretion system. We suggest that the preparation of hEx3 from bacterial insoluble material by means of in vitro refolding would be useful for industrial-scale production of the diabody for its potential use in clinical studies.

Keywords: bispecific diabody/cancer immunotherapy/EGFR/in vitro refolding/small recombinant antibody

Received February 28, 2008; revised June 5, 2008; accepted June 10, 2008.


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