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Production and characterization of anti-human interferon γ receptor antibody fragments that inhibit cytokine binding to the receptor


Bridges, Angela; Stuart, Fiona; Späth, Julia; Lang, Stefan; Henke, Christoph; Birch, Ashley; Robinson, John A (1996). Production and characterization of anti-human interferon γ receptor antibody fragments that inhibit cytokine binding to the receptor. Protein Engineering, Design & Selection, 9(4):365-370.

Abstract

Three single-chain antibody fragments that recognize the extracellular human interferon γ receptor α-chain (IFNγR), and inhibit the binding of human IFNγ, have been produced in Escherichia coli. These fragments are derived from murine anti-receptor monoclonal antibodies, and comprise the variable heavy (VH) domain linked to the variable light (VL) chain through a 15 amino acid linker [(GGGGS)3]. Using surface plasmon resonance technology (BIAcore), the soluble proteins were shown to retain a high affinity for recombinant IFNγR, and by radioimmunoassay to possess high inhibitory activity towards IFNγ-binding to human Raji cells. The antibody fragments most likely recognize epitopes that overlap the cytokine binding site on the receptor surface. Attempts to dissect further the antibodies to isolated VH- and VL-chains and to synthetic linear and cyclic peptides derived from the individual complementarity determining regions failed to afford fragments with significant IFNγR binding affinity. Nevertheless, these native-like variable region fragments and petidomimetics derived from them are of interest in the design of novel IFNγR antagonists

Abstract

Three single-chain antibody fragments that recognize the extracellular human interferon γ receptor α-chain (IFNγR), and inhibit the binding of human IFNγ, have been produced in Escherichia coli. These fragments are derived from murine anti-receptor monoclonal antibodies, and comprise the variable heavy (VH) domain linked to the variable light (VL) chain through a 15 amino acid linker [(GGGGS)3]. Using surface plasmon resonance technology (BIAcore), the soluble proteins were shown to retain a high affinity for recombinant IFNγR, and by radioimmunoassay to possess high inhibitory activity towards IFNγ-binding to human Raji cells. The antibody fragments most likely recognize epitopes that overlap the cytokine binding site on the receptor surface. Attempts to dissect further the antibodies to isolated VH- and VL-chains and to synthetic linear and cyclic peptides derived from the individual complementarity determining regions failed to afford fragments with significant IFNγR binding affinity. Nevertheless, these native-like variable region fragments and petidomimetics derived from them are of interest in the design of novel IFNγR antagonists

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Item Type:Journal Article, refereed, original work
Communities & Collections:National licences > 142-005
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Language:English
Date:1 January 1996
Deposited On:11 Oct 2018 13:49
Last Modified:12 Oct 2018 07:34
Publisher:Oxford University Press
ISSN:1741-0126
OA Status:Green
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1093/protein/9.4.365
Related URLs:https://www.swissbib.ch/Search/Results?lookfor=nationallicenceoxford101093protein94365 (Library Catalogue)

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