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J. Biochem, 2003, Vol. 133, No. 1 43-49
© 2003 Japanese Biochemical Society

BIOTECHNOLOGY

Human Fc{varepsilon}RI{alpha}–Specific Human Single-Chain Fv (scFv) Antibody with Antagonistic Activity toward IgE/Fc{varepsilon}RI{alpha}-Binding

Shuhei Hashiguchi1, Toshihiro Nakashima2, Aya Nitani1, Tomoki Yoshihara1, Keisuke Yoshinaga1, Yuji Ito1, Yoshio Maeda3 and Kazuhisa Sugimura+,1

1 Department of Bioengineering, Faculty of Engineering, Kagoshima University, 1-21-40 Korimoto, Kagoshima 890-0065; 2 The Chemo-Sero-Therapeutic Research Institute, Kyokushi Kikuchi, Kumamoto 869-1298; and 3 Kagoshima University Health Service Center, 1-21-24 Korimoto, Kagoshima 890-8580

The {alpha}-chain of Fc{varepsilon}RI (Fc{varepsilon}RI{alpha}) plays a critical role in the binding of IgE to Fc{varepsilon}RI. A fully human antibody interfering with this interaction may be useful for the prevention of IgE-mediated allergic diseases. Here, we describe the successful isolation of a human single-chain Fv antibody specific to human Fc{varepsilon}RI{alpha} using human antibody phage display libraries. Using the non-immune phage antibody libraries constructed from peripheral blood lymphocyte cDNA from 20 healthy subjects, we isolated three phage clones (designated as FcR{varepsilon}27, FcR{varepsilon}51, and FcR{varepsilon}70) through two rounds of biopanning selection. The purified soluble scFv, FcR{varepsilon}51, inhibited the binding of IgE to recombinant Fc{varepsilon}RI{alpha}, although both FcR{varepsilon}27 and FcR{varepsilon}70 showed fine binding specificity to Fc{varepsilon}RI{alpha}. Since FcR{varepsilon}51 was determined to be a monomer by HPLC, BIAcore analysis was performed. The dissociation constant of FcR{varepsilon}51 to Fc{varepsilon}RI{alpha} was estimated to be 20 nM, i.e., fortyfold lower than that of IgE binding to Fc{varepsilon}RI{alpha} (Kd = 0.5 nM). With these characteristics, FcR{varepsilon}51 exhibited inhibitory activity on the release of histamine from passively sensitized human peripheral blood mononuclear cells.

+ To whom correspondence should be addressed. Tel.: +81-99-285-8345, Fax: +81-99-258-4706, E-mail address: kazu{at}be.kagoshima-u.ac.jp


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