Identification and characterization of a novel IL-4 receptor α chain (IL-4Rα) antagonist to inhibit IL-4 signalling

Ahmed, Nayyar, Dhanapala, Pathum and Suphioglu, Cenk 2015, Identification and characterization of a novel IL-4 receptor α chain (IL-4Rα) antagonist to inhibit IL-4 signalling, Cellular physiology and biochemistry, vol. 36, no. 3, pp. 831-842, doi: 10.1159/000430259.

Attached Files
Name Description MIMEType Size Downloads

Title Identification and characterization of a novel IL-4 receptor α chain (IL-4Rα) antagonist to inhibit IL-4 signalling
Author(s) Ahmed, Nayyar
Dhanapala, Pathum
Suphioglu, CenkORCID iD for Suphioglu, Cenk
Journal name Cellular physiology and biochemistry
Volume number 36
Issue number 3
Start page 831
End page 842
Total pages 12
Publisher Karger
Place of publication Basal, Switzerland
Publication date 2015
ISSN 1421-9778
Keyword(s) Alkaline Phosphatase
Anti-Allergic Agents
Biological Assay
Cell Line
Gene Expression
HEK293 Cells
Interleukin-4 Receptor alpha Subunit
Peptide Library
Protein Binding
Protein Isoforms
Signal Transduction
Science & Technology
Life Sciences & Biomedicine
Cell Biology
Phage display
IL-4 signalling pathway
IL-4 receptor
HEK-Blue cell line
Summary BACKGROUND/AIMS: In recent times, allergy has become a financial, physical and psychological burden to the society as a whole. In allergic cascades, cytokine IL-4 binds to IL-4 receptor (IL-4R), consequently producing allergen-specific IgE antibodies by B cells. In addition, among other functions, IL-4 is also responsible for B and T cell proliferation and differentiation. Hence, characterization of novel antagonists that inhibit IL-4 signalling forms the overall aim of this study. METHODS: Phage display was used to screen a random 12-mer synthetic peptide library with a human IL-4Rα to identify peptide candidates. Once identified, the peptides were commercially synthesized and used for in vitro immunoassays. RESULTS: We have successfully used phage display to identify M13 phage clones that demonstrated specific binding to IL-4Rα. The peptide N1 was synthesized for use in ELISA, demonstrating significant binding to IL-4Rα and inhibiting interaction with cytokine IL-4. Furthermore, the peptide was tested in a transfected HEK-Blue IL-4 reporter cell line model, which produces alkaline phosphatase (AP). QUANTI-Blue, a substrate, breaks down in the presence of AP producing a blue coloration. Using this colorimetric analysis, >50% inhibition of IL-4 signalling was achieved. CONCLUSION: We have successfully identified and characterised a synthetic peptide antagonist against IL-4Rα, which effectively inhibits IL-4 interaction with the IL-4Rα in vitro. Since IL-4 interaction with IL-4Rα is a common pathway for many allergies, a prophylactic treatment can be devised by inhibiting this interaction for future treatment of allergies.
Language eng
DOI 10.1159/000430259
Field of Research 060804 Animal Immunology
1116 Medical Physiology
Socio Economic Objective 970106 Expanding Knowledge in the Biological Sciences
HERDC Research category C1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2015, Karger
Persistent URL

Connect to link resolver
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 2 times in TR Web of Science
Scopus Citation Count Cited 2 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 264 Abstract Views, 1 File Downloads  -  Detailed Statistics
Created: Tue, 19 Jul 2016, 14:59:36 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact