Production of biologically active IgG hinge-tag soluble epidermal growth factor receptors (ErbB)

Takayuki Otani; Toshihiro Hashizume; Tadahiro Nagaoka; Tomoko Fukuda; Careen K. Tang; David S. Salomon; Masaharu Seno

doi:10.1007/s10529-009-0160-9

Production of biologically active IgG hinge-tag soluble epidermal growth factor receptors (ErbB)

Takayuki Otani
, Toshihiro Hashizume
, Tadahiro Nagaoka
, Tomoko Fukuda
, Careen K. Tang
, David S. Salomon
, Masaharu Seno

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

1 Citation (Scopus)

Abstract

The extracellular domains (ECD) of epidermal growth factor receptors, ErbB1, 2, 3 and 4, were designed as soluble dimeric forms. Each ECD was fused to a short hinge region derived from IgG, such that the stable dimer could be formed with disulfide bridges. This hinge-tagged design minimized the molecular weight to approximately 50% of the conventional Fc-fusion design without an Fc domain of IgG. The refolded dimers could be easily analyzed and characterized by SDS-PAGE. Hinge-tagged soluble ErbBs demonstrated significant affinity for betacellulin and heregulin. The IgG hinge-tag should be a simple method to design soluble dimers that would be useful for high throughput screening of ligands, antagonists or derivatives.

Original language	English
Pages (from-to)	361-366
Number of pages	6
Journal	Biotechnology Letters
Volume	32
Issue number	3
DOIs	https://doi.org/10.1007/s10529-009-0160-9
Publication status	Published - 02-2010
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1007/s10529-009-0160-9

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@article{61b4a45d42c9467b890b9802213882ee,

title = "Production of biologically active IgG hinge-tag soluble epidermal growth factor receptors (ErbB)",

abstract = "The extracellular domains (ECD) of epidermal growth factor receptors, ErbB1, 2, 3 and 4, were designed as soluble dimeric forms. Each ECD was fused to a short hinge region derived from IgG, such that the stable dimer could be formed with disulfide bridges. This hinge-tagged design minimized the molecular weight to approximately 50\% of the conventional Fc-fusion design without an Fc domain of IgG. The refolded dimers could be easily analyzed and characterized by SDS-PAGE. Hinge-tagged soluble ErbBs demonstrated significant affinity for betacellulin and heregulin. The IgG hinge-tag should be a simple method to design soluble dimers that would be useful for high throughput screening of ligands, antagonists or derivatives.",

author = "Takayuki Otani and Toshihiro Hashizume and Tadahiro Nagaoka and Tomoko Fukuda and Tang, \{Careen K.\} and Salomon, \{David S.\} and Masaharu Seno",

note = "Funding Information: Acknowledgements We thank Ms. N. Hironaka for the construction of sErbB2 and sErbB3 expression plasmid. This research was partly supported by the Ministry of Education, Culture, Sports, Science and Technology Grant-in-Aid for Scientific Research (B) Nos. 18300164 and 21300179.",

year = "2010",

month = feb,

doi = "10.1007/s10529-009-0160-9",

language = "English",

volume = "32",

pages = "361--366",

journal = "Biotechnology Letters",

issn = "0141-5492",

publisher = "Springer Science and Business Media B.V.",

number = "3",

}

TY - JOUR

T1 - Production of biologically active IgG hinge-tag soluble epidermal growth factor receptors (ErbB)

AU - Otani, Takayuki

AU - Hashizume, Toshihiro

AU - Nagaoka, Tadahiro

AU - Fukuda, Tomoko

AU - Tang, Careen K.

AU - Salomon, David S.

AU - Seno, Masaharu

N1 - Funding Information: Acknowledgements We thank Ms. N. Hironaka for the construction of sErbB2 and sErbB3 expression plasmid. This research was partly supported by the Ministry of Education, Culture, Sports, Science and Technology Grant-in-Aid for Scientific Research (B) Nos. 18300164 and 21300179.

PY - 2010/2

Y1 - 2010/2

N2 - The extracellular domains (ECD) of epidermal growth factor receptors, ErbB1, 2, 3 and 4, were designed as soluble dimeric forms. Each ECD was fused to a short hinge region derived from IgG, such that the stable dimer could be formed with disulfide bridges. This hinge-tagged design minimized the molecular weight to approximately 50% of the conventional Fc-fusion design without an Fc domain of IgG. The refolded dimers could be easily analyzed and characterized by SDS-PAGE. Hinge-tagged soluble ErbBs demonstrated significant affinity for betacellulin and heregulin. The IgG hinge-tag should be a simple method to design soluble dimers that would be useful for high throughput screening of ligands, antagonists or derivatives.

AB - The extracellular domains (ECD) of epidermal growth factor receptors, ErbB1, 2, 3 and 4, were designed as soluble dimeric forms. Each ECD was fused to a short hinge region derived from IgG, such that the stable dimer could be formed with disulfide bridges. This hinge-tagged design minimized the molecular weight to approximately 50% of the conventional Fc-fusion design without an Fc domain of IgG. The refolded dimers could be easily analyzed and characterized by SDS-PAGE. Hinge-tagged soluble ErbBs demonstrated significant affinity for betacellulin and heregulin. The IgG hinge-tag should be a simple method to design soluble dimers that would be useful for high throughput screening of ligands, antagonists or derivatives.

UR - https://www.scopus.com/pages/publications/77649338416

UR - https://www.scopus.com/pages/publications/77649338416#tab=citedBy

U2 - 10.1007/s10529-009-0160-9

DO - 10.1007/s10529-009-0160-9

M3 - Article

C2 - 19898750

AN - SCOPUS:77649338416

SN - 0141-5492

VL - 32

SP - 361

EP - 366

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 3

ER -

Production of biologically active IgG hinge-tag soluble epidermal growth factor receptors (ErbB)

Abstract

All Science Journal Classification (ASJC) codes

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