Optimization of the inter-domain structure of galectin-9 for recombinant production

Aiko Itoh, Yoko Fukata, Hiroshi Miyanaka, Yasuhiro Nonaka, Takashi Ogawa, Takanori Nakamura, Nozomu Nishi

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6 Citations (Scopus)


We previously developed a stable form of galectin-9, an immunomodulatory animal lectin with a truncated linker peptide (G9Null), to overcome the protease sensitivity of wild-type galectin-9. G9Null is highly resistant to proteolysis, while the modification marginally improved the low solubility of the wild-type protein. To increase its solubility, we further modified the remaining linker region of G9Null. A 10-amino acid deletion with a single amino acid substitution resulted in an ∼400% increase in solubility and yield without an adverse effect on its biological activity. This mutant protein might be useful for large-scale recombinant production needed for evaluation of the therapeutic potential of galectin-9.

Original languageEnglish
Pages (from-to)920-925
Number of pages6
Issue number8
Publication statusPublished - Aug 1 2013


All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Itoh, A., Fukata, Y., Miyanaka, H., Nonaka, Y., Ogawa, T., Nakamura, T., & Nishi, N. (2013). Optimization of the inter-domain structure of galectin-9 for recombinant production. Glycobiology, 23(8), 920-925. https://doi.org/10.1093/glycob/cwt023