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Journal of Biomolecular Screening
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Neutralizing Antibodies of Botulinum Neurotoxin Serotype A Screened from a Fully Synthetic Human Antibody Phage Display Library

Rui Yu

Beijing Institute of Biotechnology, Beijing, China

Shuang Wang

Beijing Institute of Biotechnology, Beijing, China, wangsshuang{at}tom.com, szwyhhh{at}yahoo.com.cn

Yun-zhou Yu

Beijing Institute of Biotechnology, Beijing, China

Wei-shi Du

Beijing Institute of Biotechnology, Beijing, China

Fang Yang

Beijing Institute of Biotechnology, Beijing, China

Wei-yuan Yu

Beijing Institute of Biotechnology, Beijing, China

Zhi-wei Sun

Beijing Institute of Biotechnology, Beijing, China

The botulinum neurotoxins (BoNTs) produced by Clostridium botulinum are the most poisonous protein substances known. The neutralizing antibodies against botulinum neurotoxin can effectively prevent and cure the toxicosis. Using purified Hc fragments of botulinum neurotoxin serotype A (BoNT/A-Hc) as antigen, 2 specific neutralizing antibodies mapping different epitopes were selected from a fully synthetic human antibody library. The 2 antibodies can effectively inhibit the binding between BoNT/A-Hc and differentiated PC-12 cells in vitro, and the neutralization was evaluated in vivo. Although no single mAb completely protected mice from toxin, they both could prolong time to death when challenged with 20 LD 50s (50% lethal doses) of BoNT/A. When used together, the mAbs completely neutralized 1000 LD50s/mg Ab, suggesting their high neutralizing potency in vivo. The results would lead to further production of neutralizing antibody drugs against BoNT/A. It also proved that it was a quick method to obtain human therapeutic antibodies by selecting from the fully synthetic human antibody phage display library. (Journal of Biomolecular Screening 2009:991-998)

Key Words: botulinum neurotoxins • Hc fragment • neutralizing antibody • fully synthetic human antibody library • phage display

This version was published on September 1, 2009

Journal of Biomolecular Screening, Vol. 14, No. 8, 991-998 (2009)
DOI: 10.1177/1087057109343206
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