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International Immunology Advance Access published online on December 16, 2005
International Immunology, doi:10.1093/intimm/dxh338
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© The Japanese Society for Immunology. 2005. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received March 10, 2005
Accepted September 16, 2005

Article

Identification of core functional region of murine IL-4 using peptide phage display and molecular modeling

Gang Yao 1, Weiyan Chen 2, Haibin Luo 3, Qunfeng Jiang 1, Zongxiang Xia 2, Lei Zang 1, Jianping Zuo 3, Xin Wei 4, Zhengjun Chen 1, Xu Shen 3, Chen Dong 5, and Bing Sun 6 *

1 Laboratory of Molecular Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institute for Biological Sciences, Chinese Academy of Sciences, 320 Yueyang Road, Shanghai 200031, China
2 State Key Laboratory of Bio-organic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China
3 Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 201203, China
4 GL Biochem (Shanghai) Ltd, 351 Guo Shoujing Road, Shanghai 201203, China
5 Department of Immunology, MD Anderson Cancer Center, 7455 Fannin, Unit 902, Houston, TX 77030-1903, USA
6 Laboratory of Molecular Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institute for Biological Sciences, Chinese Academy of Sciences, 320 Yueyang Road, Shanghai 200031, China; Immunology Division, E-Institutes of Shanghai Universities

* To whom correspondence should be addressed.
Bing Sun, E-mail: bsun{at}sibs.ac.cn


  Abstract

Murine IL-4 is a pleiotropic cytokine with undefined core functional region for eliciting downstream signaling. We used molecular modeling to predict the binding sites recognized by an anti-IL-4-neutralizing mAb (11B.11) and peptide phage display to delineate their makeup. The results of these approaches were confirmed by site-directed mutagenesis analysis. The results suggest that the amino acid residues spanning from 79 to 86 (QRLFRAFR) on IL-4 are of the major binding site for 11B.11. Furthermore, the functional experiments demonstrate that the residues R80, R83 and R86, which are located in the helix C of murine IL-4, play a crucial role in binding to the IL-4R {alpha}-chain. Taken together, a new core functional region of murine IL-4 is identified, which provides new insight into the interaction between IL-4 and IL-4R{alpha}. In addition, the results demonstrate that 11B.11 binds to a core functional region of murine IL-4, which prevents this cytokine from interacting with its cognate receptor.

Keywords: 11B.11; core functional region of IL-4; IL-4; molecular modeling; peptide phage display.
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