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

doi:10.1093/protein/4.7.837

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)

University of Helsinki

Research output: Contribution to journal › Article › Scientific › peer-review

107 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 language	English
Pages (from-to)	837 - 841
Number of pages	5
Journal	Protein Engineering
Volume	4
Issue number	7
DOIs	https://doi.org/10.1093/protein/4.7.837
Publication status	Published - 1991
MoE publication type	A1 Journal article-refereed

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

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.",

author = "Kristiina Takkinen and Marja-Leena Laukkanen and Dorothea Sizmann and Kaija Alfthan and Tiina Immonen and Liisa Vanne and Matti Kaartinen and Jonathan Knowles and Tuula Teeri",

note = "Project code: BIO8015",

year = "1991",

doi = "10.1093/protein/4.7.837",

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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

SN - 0269-2139

VL - 4

SP - 837

EP - 841

JO - Protein Engineering

JF - Protein Engineering

IS - 7

ER -

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

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