AN ACTIVE SINGLE-CHAIN ANTIBODY CONTAINING A CELLULASE LINKER DOMAIN IS SECRETED BY ESCHERICHIA-COLI

K TAKKINEN; ML LAUKKANEN; D SIZMANN; K ALFTHAN; T IMMONEN; L VANNE; Matti Kaartinen; JKC KNOWLES; Tuula T. Teeri

AN ACTIVE SINGLE-CHAIN ANTIBODY CONTAINING A CELLULASE LINKER DOMAIN IS SECRETED BY ESCHERICHIA-COLI

K TAKKINEN, ML LAUKKANEN, D SIZMANN, K ALFTHAN, T IMMONEN, L VANNE, Matti Kaartinen, JKC KNOWLES, Tuula T. Teeri

Not published at Aalto University

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

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 IgG1 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/l 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
Publication status	Published - Oct 1991
MoE publication type	A1 Journal article-refereed

Keywords

CELLULASE LINKER PEPTIDE
ESCHERICHIA-COLI
EXTRACELLULAR PRODUCTION
SINGLE-CHAIN ANTIBODY
VARIABLE DOMAINS
X-RAY-SCATTERING
TRICHODERMA-REESEI
CELLOBIOHYDROLASE-II
PROTEINS
GENE
EXPRESSION
SEQUENCE
VECTORS
FRAGMENT
PRODUCT

Cite this

@article{e23fcf6a676848b4b6f7a0f5c43212bc,

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 IgG1 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/l of culture medium and its affinity and stability are comparable to those of the corresponding native IgG.",

keywords = "CELLULASE LINKER PEPTIDE, ESCHERICHIA-COLI, EXTRACELLULAR PRODUCTION, SINGLE-CHAIN ANTIBODY, VARIABLE DOMAINS, X-RAY-SCATTERING, TRICHODERMA-REESEI, CELLOBIOHYDROLASE-II, PROTEINS, GENE, EXPRESSION, SEQUENCE, VECTORS, FRAGMENT, PRODUCT",

author = "K TAKKINEN and ML LAUKKANEN and D SIZMANN and K ALFTHAN and T IMMONEN and L VANNE and Matti Kaartinen and JKC KNOWLES and Teeri, {Tuula T.}",

year = "1991",

month = oct,

language = "English",

volume = "4",

pages = "837--841",

journal = "PROTEIN ENGINEERING",

issn = "0269-2139",

number = "7",

}

TY - JOUR

T1 - AN ACTIVE SINGLE-CHAIN ANTIBODY CONTAINING A CELLULASE LINKER DOMAIN IS SECRETED BY ESCHERICHIA-COLI

AU - TAKKINEN, K

AU - LAUKKANEN, ML

AU - SIZMANN, D

AU - ALFTHAN, K

AU - IMMONEN, T

AU - VANNE, L

AU - Kaartinen, Matti

AU - KNOWLES, JKC

AU - Teeri, Tuula T.

PY - 1991/10

Y1 - 1991/10

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 IgG1 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/l 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 IgG1 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/l of culture medium and its affinity and stability are comparable to those of the corresponding native IgG.

KW - CELLULASE LINKER PEPTIDE

KW - ESCHERICHIA-COLI

KW - EXTRACELLULAR PRODUCTION

KW - SINGLE-CHAIN ANTIBODY

KW - VARIABLE DOMAINS

KW - X-RAY-SCATTERING

KW - TRICHODERMA-REESEI

KW - CELLOBIOHYDROLASE-II

KW - PROTEINS

KW - GENE

KW - EXPRESSION

KW - SEQUENCE

KW - VECTORS

KW - FRAGMENT

KW - PRODUCT

M3 - Article

VL - 4

SP - 837

EP - 841

JO - PROTEIN ENGINEERING

JF - PROTEIN ENGINEERING

SN - 0269-2139

IS - 7

ER -