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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Single-Chain Antibodies
Cellulase
Antibodies
Escherichia coli
Culture Media
Peptides
Polypeptides
Antigens
Immunoglobulin G

Cite this

Takkinen, Kristiina ; Laukkanen, Marja-Leena ; Sizmann, Dorothea ; Alfthan, Kaija ; Immonen, Tiina ; Vanne, Liisa ; Kaartinen, Matti ; Knowles, Jonathan ; Teeri, Tuula. / An active single-chain antibody containing a cellulase linker domain is secreted by Escherichia coli. In: Protein Engineering. 1991 ; Vol. 4, No. 7. pp. 837 - 841.
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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.",
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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, vol. 4, no. 7, pp. 837 - 841. https://doi.org/10.1093/protein/4.7.837

An active single-chain antibody containing a cellulase linker domain is secreted by Escherichia coli. / Takkinen, Kristiina; Laukkanen, Marja-Leena; Sizmann, Dorothea; Alfthan, Kaija; Immonen, Tiina; Vanne, Liisa; Kaartinen, Matti; Knowles, Jonathan; Teeri, Tuula (Corresponding Author).

In: Protein Engineering, Vol. 4, No. 7, 1991, p. 837 - 841.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - An active single-chain antibody containing a cellulase linker domain is secreted by Escherichia coli

AU - Takkinen, Kristiina

AU - Laukkanen, Marja-Leena

AU - Sizmann, Dorothea

AU - Alfthan, Kaija

AU - Immonen, Tiina

AU - Vanne, Liisa

AU - Kaartinen, Matti

AU - Knowles, Jonathan

AU - Teeri, Tuula

N1 - Project code: BIO8015

PY - 1991

Y1 - 1991

N2 - 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.

AB - 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.

U2 - 10.1093/protein/4.7.837

DO - 10.1093/protein/4.7.837

M3 - Article

VL - 4

SP - 837

EP - 841

JO - Protein Engineering, Design and Selection

JF - Protein Engineering, Design and Selection

SN - 1741-0126

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ER -