An active single-chain antibody containing a cellulase linker domain is secreted by Escherichia coli

Kristiina Takkinen, Marja-Leena Laukkanen, Dorothea Sizmann, Kaija Alfthan, Tiina Immonen, Liisa Vanne, Matti Kaartinen, Jonathan Knowles, Tuula Teeri (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

92 Citations (Scopus)

Abstract

Single-chain antibodies consist of the variable, antigen-binding domains of antibodies joined to a continuous polypeptide by genetically engineered peptide linkers. We have used the flexible interdomain linker region of a fungal cellulase to link together the variable domains of an anti-2-phenyloxazolone IgGl and show here that the resulting single-chain antibody is efficiently secreted and released to the culture medium of Escherichia coli. The yield of affinity-purified single-chain antibody is 1 -2 mg/1 of culture medium and its affinity and stability are comparable to those of the corresponding native IgG.

Original languageEnglish
Pages (from-to)837 - 841
Number of pages5
JournalProtein Engineering
Volume4
Issue number7
DOIs
Publication statusPublished - 1991
MoE publication typeA1 Journal article-refereed

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    Takkinen, K., Laukkanen, M-L., Sizmann, D., Alfthan, K., Immonen, T., Vanne, L., Kaartinen, M., Knowles, J., & Teeri, T. (1991). An active single-chain antibody containing a cellulase linker domain is secreted by Escherichia coli. Protein Engineering, 4(7), 837 - 841. https://doi.org/10.1093/protein/4.7.837