Neutralization and binding activity of a human single-chain antibody to ricin toxin

Abstract

Ricin toxin (RT), extracted from castor bean, is a type II ribosome-inactivating protein (RIP). As a biothreat agent, there is no effective antidote for RT to date, but recent advances in antibody research may have meet this need. This study aimed to produce human single-chain antibody variable fragments (HuscFvs) that bind to and interfere with RT activity for further clinical use. The purified RT component was used in phage biopanning to select ricin-bound HuscFv-displayed phage clones from synthetic (Tomlinson I + J) phage display libraries. The selected HuscFv, named JE11, showed an almost 100% protective effect to HeLa cells by mixing with RT at a 1:1000 ratio in vitro. The antibody showed an 83% protection against injection of 2 × LD50 RT dose mice within 72 h. This research has therapeutic potential for the diagnosis and treatment of RT poisoning.

Keywords

• ricin toxin
• human single-chain antibody variable fragments (huscfvs)
• phage library